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PDBsum entry 1g0u
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protein metals Protein-protein interface(s) links
Hydrolase PDB id
1g0u

 

 

 

 

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Contents
Protein chains
246 a.a. *
235 a.a. *
238 a.a. *
230 a.a. *
230 a.a. *
242 a.a. *
240 a.a. *
222 a.a. *
204 a.a. *
198 a.a. *
212 a.a. *
222 a.a. *
233 a.a. *
196 a.a. *
Metals
_MG ×20
Waters ×2908
* Residue conservation analysis
PDB id:
1g0u
Name: Hydrolase
Title: A gated channel into the proteasome core particle
Structure: Proteasome component y7. Chain: a, o. Synonym: macropain subunit y7, proteinase ysce subunit 7, multicatalytic endopeptidase complex subunit y7. Other_details: part of 20s subunit. Proteasome component y13. Chain: b, p. Synonym: macropain subunit y13, proteinase ysce subunit 13, multicatalytic endopeptidase complex subunit y13.
Source: Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Variant: sub61. Variant: sub61
Biol. unit: 28mer (from PQS)
Resolution:
2.40Å     R-factor:   0.250     R-free:   0.303
Authors: M.Groll,M.Bajorek,A.Kohler,L.Moroder,D.M.Rubin,R.Huber,M.H.Glickman, D.Finley
Key ref:
M.Groll et al. (2000). A gated channel into the proteasome core particle. Nat Struct Biol, 7, 1062-1067. PubMed id: 11062564 DOI: 10.1038/80992
Date:
09-Oct-00     Release date:   06-Nov-00    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P23639  (PSA2_YEAST) -  Proteasome subunit alpha type-2 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Seq:
Struc: 		250 a.a.
246 a.a.
Protein chains
Pfam   ArchSchema ?
P23638  (PSA3_YEAST) -  Proteasome subunit alpha type-3 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Seq:
Struc: 		258 a.a.
235 a.a.
Protein chains
Pfam   ArchSchema ?
P40303  (PSA4_YEAST) -  Proteasome subunit alpha type-4 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Seq:
Struc: 		254 a.a.
238 a.a.
Protein chains
Pfam   ArchSchema ?
P32379  (PSA5_YEAST) -  Proteasome subunit alpha type-5 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Seq:
Struc: 		260 a.a.
230 a.a.*
Protein chains
Pfam   ArchSchema ?
P40302  (PSA6_YEAST) -  Proteasome subunit alpha type-6 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Seq:
Struc: 		234 a.a.
230 a.a.*
Protein chains
Pfam   ArchSchema ?
P21242  (PSA7_YEAST) -  Probable proteasome subunit alpha type-7 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Seq:
Struc: 		288 a.a.
242 a.a.
Protein chains
Pfam   ArchSchema ?
P21243  (PSA1_YEAST) -  Proteasome subunit alpha type-1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Seq:
Struc: 		252 a.a.
240 a.a.
Protein chains
Pfam   ArchSchema ?
P25043  (PSB2_YEAST) -  Proteasome subunit beta type-2 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Seq:
Struc: 		261 a.a.
222 a.a.
Protein chains
Pfam   ArchSchema ?
P25451  (PSB3_YEAST) -  Proteasome subunit beta type-3 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Seq:
Struc: 		205 a.a.
204 a.a.
Protein chains
Pfam   ArchSchema ?
P22141  (PSB4_YEAST) -  Proteasome subunit beta type-4 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Seq:
Struc: 		198 a.a.
198 a.a.
Protein chains
Pfam   ArchSchema ?
P30656  (PSB5_YEAST) -  Proteasome subunit beta type-5 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Seq:
Struc: 		287 a.a.
212 a.a.
Protein chains
Pfam   ArchSchema ?
P23724  (PSB6_YEAST) -  Proteasome subunit beta type-6 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Seq:
Struc: 		241 a.a.
222 a.a.
Protein chains
Pfam   ArchSchema ?
P30657  (PSB7_YEAST) -  Proteasome subunit beta type-7 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Seq:
Struc: 		266 a.a.
233 a.a.
Protein chains
Pfam   ArchSchema ?
P38624  (PSB1_YEAST) -  Proteasome subunit beta type-1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Seq:
Struc: 		215 a.a.
196 a.a.
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 4 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class 2: Chains A, B, C, D, E, F, G, I, J, L, M, O, P, Q, R, S, T, U, W, X, Z, 1: E.C.3.4.99.46  - Transferred entry: 3.4.25.1.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
   Enzyme class 3: Chains H, K, N, V, Y, 2: E.C.3.4.25.1  - proteasome endopeptidase complex.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Cleavage at peptide bonds with very broad specificity.
Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

 

 
DOI no: 10.1038/80992 Nat Struct Biol 7:1062-1067 (2000)
PubMed id: 11062564  
 
 
A gated channel into the proteasome core particle.
M.Groll, M.Bajorek, A.Köhler, L.Moroder, D.M.Rubin, R.Huber, M.H.Glickman, D.Finley.
 
  ABSTRACT  
 
The core particle (CP) of the yeast proteasome is composed of four heptameric rings of subunits arranged in a hollow, barrel-like structure. We report that the CP is autoinhibited by the N-terminal tails of the outer (alpha) ring subunits. Crystallographic analysis showed that deletion of the tail of the alpha 3-subunit opens a channel into the proteolytically active interior chamber of the CP, thus derepressing peptide hydrolysis. In the latent state of the particle, the tails prevent substrate entry by imposing topological closure on the CP. Inhibition by the alpha-subunit tails is relieved upon binding of the regulatory particle to the CP to form the proteasome holoenzyme.
 
  Selected figure(s)  
 
Figure 4.
Figure 4. Contacts among residues of the YDR element in adjacent tails. Detail of the CP channel in the closed state, showing that the carboxylate group of Asp 9 in 3 forms a salt bridge with the guanidinium group of Arg 10 in 4, and a hydrogen bond with the hydroxyl group of Tyr 8 in 4. The carboxylate group of Asp 9 also forms hydrogen bonds with the 3 main chain, as shown. 		Figure 5.
Figure 5. Model for coupled regulation of proteasome assembly and inhibition. Proposed late steps in the assembly of the proteasome are depicted. The inhibitory N-terminal sequences of the -subunits and -subunits are represented in red. In the inactive half-CP, inhibition is provided by the -subunit propeptides (which directly block the proteolytic active sites). Inhibition by the -subunit tails becomes effective only when the half-CPs condense to form a closed chamber. The inactive CP is converted to the latent form upon autolysis of the -propeptides. The last step represents holoenzyme formation, which is accompanied by channel opening. For details, see the text. RP, regulatory particle. The schematic representation of -propeptide-mediated inhibition is modified from ref. 20.
 
  The above figures are reprinted by permission from Macmillan Publishers Ltd: Nat Struct Biol (2000, 7, 1062-1067) copyright 2000.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21499243 A.R.Kusmierczyk, M.J.Kunjappu, R.Y.Kim, and M.Hochstrasser (2011).
A conserved 20S proteasome assembly factor requires a C-terminal HbYX motif for proteasomal precursor binding.
  Nat Struct Mol Biol, 18, 622-629.  
  21304520 C.Heinen, K.Acs, D.Hoogstraten, and N.P.Dantuma (2011).
C-terminal UBA domains protect ubiquitin receptors by preventing initiation of protein degradation.
  Nat Commun, 2, 191.  
21387144 E.J.Sijts, and P.M.Kloetzel (2011).
The role of the proteasome in the generation of MHC class I ligands and immune responses.
  Cell Mol Life Sci, 68, 1491-1502.  
22037170 G.Tian, S.Park, M.J.Lee, B.Huck, F.McAllister, C.P.Hill, S.P.Gygi, and D.Finley (2011).
An asymmetric interface between the regulatory and core particles of the proteasome.
  Nat Struct Mol Biol, 18, 1259-1267.  
21484190 L.J.Crawford, B.Walker, and A.E.Irvine (2011).
Proteasome inhibitors in cancer therapy.
  J Cell Commun Signal, 5, 101-110.  
20061387 A.Chandra, L.Chen, H.Liang, and K.Madura (2010).
Proteasome assembly influences interaction with ubiquitinated proteins and shuttle factors.
  J Biol Chem, 285, 8330-8339.  
19760349 A.Voigt, K.Bartel, K.Egerer, C.Trimpert, E.Feist, C.Gericke, R.Kandolf, K.Klingel, U.Kuckelkorn, K.Stangl, S.B.Felix, G.Baumann, P.M.Kloetzel, and A.Staudt (2010).
Humoral anti-proteasomal autoimmunity in dilated cardiomyopathy.
  Basic Res Cardiol, 105, 9.  
20305655 B.G.Lee, E.Y.Park, K.E.Lee, H.Jeon, K.H.Sung, H.Paulsen, H.Rübsamen-Schaeff, H.Brötz-Oesterhelt, and H.K.Song (2010).
Structures of ClpP in complex with acyldepsipeptide antibiotics reveal its activation mechanism.
  Nat Struct Mol Biol, 17, 471-478.
PDB codes: 3ktg 3kth 3kti 3ktj 3ktk
21125340 J.J.Driscoll, and R.Dechowdhury (2010).
Therapeutically targeting the SUMOylation, Ubiquitination and Proteasome pathways as a novel anticancer strategy.
  Target Oncol, 5, 281-289.  
20541423 N.Gallastegui, and M.Groll (2010).
The 26S proteasome: assembly and function of a destructive machine.
  Trends Biochem Sci, 35, 634-642.  
19633314 N.P.Dantuma, and K.Lindsten (2010).
Stressing the ubiquitin-proteasome system.
  Cardiovasc Res, 85, 263-271.  
19684034 O.Tsukamoto, T.Minamino, and M.Kitakaze (2010).
Functional alterations of cardiac proteasomes under physiological and pathological conditions.
  Cardiovasc Res, 85, 339-346.  
19793765 S.R.Powell, and A.Divald (2010).
The ubiquitin-proteasome system in myocardial ischaemia and preconditioning.
  Cardiovasc Res, 85, 303-311.  
20019667 Y.Yu, D.M.Smith, H.M.Kim, V.Rodriguez, A.L.Goldberg, and Y.Cheng (2010).
Interactions of PAN's C-termini with archaeal 20S proteasome and implications for the eukaryotic proteasome-ATPase interactions.
  EMBO J, 29, 692-702.
PDB code: 3ipm
19812037 A.Navon, and A.Ciechanover (2009).
The 26 S proteasome: from basic mechanisms to drug targeting.
  J Biol Chem, 284, 33713-33718.  
20005843 A.Peth, H.C.Besche, and A.L.Goldberg (2009).
Ubiquitinated proteins activate the proteasome by binding to Usp14/Ubp6, which causes 20S gate opening.
  Mol Cell, 36, 794-804.  
19169257 D.Bech-Otschir, A.Helfrich, C.Enenkel, G.Consiglieri, M.Seeger, H.G.Holzhütter, B.Dahlmann, and P.M.Kloetzel (2009).
Polyubiquitin substrates allosterically activate their own degradation by the 26S proteasome.
  Nat Struct Mol Biol, 16, 219-225.  
19489727 D.Finley (2009).
Recognition and processing of ubiquitin-protein conjugates by the proteasome.
  Annu Rev Biochem, 78, 477-513.  
19589775 D.Thompson, K.Hakala, and G.N.DeMartino (2009).
Subcomplexes of PA700, the 19 S regulator of the 26 S proteasome, reveal relative roles of AAA subunits in 26 S proteasome assembly and activation and ATPase activity.
  J Biol Chem, 284, 24891-24903.  
19841631 E.K.Schrader, K.G.Harstad, and A.Matouschek (2009).
Targeting proteins for degradation.
  Nat Chem Biol, 5, 815-822.  
19639565 G.Chen, Y.Luo, X.Wang, Z.Zhao, H.Liu, H.Zhang, and Z.Li (2009).
A relatively simple and economical protocol for proteomic analyses of human 20S proteasome: Compatible with both scaled-up and scaled-down purifications.
  Electrophoresis, 30, 2422-2430.  
19282181 G.N.DeMartino (2009).
PUPylation: something old, something new, something borrowed, something Glu.
  Trends Biochem Sci, 34, 155-158.  
19277057 J.M.Belote, and L.Zhong (2009).
Duplicated proteasome subunit genes in Drosophila and their roles in spermatogenesis.
  Heredity, 103, 23-31.  
19054805 K.Yabe, and T.Koide (2009).
Inhibition of the 20S Proteosome by a Protein Proteinase Inhibitor: Evidence That a Natural Serine Proteinase Inhibitor Can Inhibit a Threonine Proteinase.
  J Biochem, 145, 217-227.  
18971267 K.Yuksek, W.L.Chen, D.Chien, and J.H.Ou (2009).
Ubiquitin-independent degradation of hepatitis C virus F protein.
  J Virol, 83, 612-621.  
19365565 L.Gustafsson, S.Aits, P.Onnerfjord, M.Trulsson, P.Storm, and C.Svanborg (2009).
Changes in proteasome structure and function caused by HAMLET in tumor cells.
  PLoS ONE, 4, e5229.  
19376868 M.A.Humbard, G.Zhou, and J.A.Maupin-Furlow (2009).
The N-terminal penultimate residue of 20S proteasome alpha1 influences its N(alpha) acetylation and protein levels as well as growth rate and stress responses of Haloferax volcanii.
  J Bacteriol, 191, 3794-3803.  
19363223 N.Medalia, A.Beer, P.Zwickl, O.Mihalache, M.Beck, O.Medalia, and A.Navon (2009).
Architecture and molecular mechanism of PAN, the archaeal proteasome regulatory ATPase.
  J Biol Chem, 284, 22952-22960.  
19679091 P.A.Osmulski, M.Hochstrasser, and M.Gaczynska (2009).
A tetrahedral transition state at the active sites of the 20S proteasome is coupled to opening of the alpha-ring channel.
  Structure, 17, 1137-1147.  
19345208 Q.Li, X.Zhao, L.J.Zhong, H.Y.Yang, Q.Wang, and X.P.Pu (2009).
Effects of chronic morphine treatment on protein expression in rat dorsal root ganglia.
  Eur J Pharmacol, 612, 21-28.  
19165213 S.Murata, H.Yashiroda, and K.Tanaka (2009).
Molecular mechanisms of proteasome assembly.
  Nat Rev Mol Cell Biol, 10, 104-115.  
19254626 S.V.Rajkumar (2009).
Multiple myeloma.
  Curr Probl Cancer, 33, 7.  
19286367 Y.Cheng (2009).
Toward an atomic model of the 26S proteasome.
  Curr Opin Struct Biol, 19, 203-208.  
19178136 Y.Kim, K.Kang, I.Kim, Y.J.Lee, C.Oh, J.Ryoo, E.Jeong, and K.Ahn (2009).
Molecular mechanisms of MHC class I-antigen processing: redox considerations.
  Antioxid Redox Signal, 11, 907-936.  
19500299 Y.Sonoda, K.Sako, Y.Maki, N.Yamazaki, H.Yamamoto, A.Ikeda, and J.Yamaguchi (2009).
Regulation of leaf organ size by the Arabidopsis RPT2a 19S proteasome subunit.
  Plant J, 60, 68-78.  
18927584 A.Lehmann, K.Jechow, and C.Enenkel (2008).
Blm10 binds to pre-activated proteasome core particles with open gate conformation.
  EMBO Rep, 9, 1237-1243.  
18713001 A.R.Kusmierczyk, and M.Hochstrasser (2008).
Some assembly required: dedicated chaperones in eukaryotic proteasome biogenesis.
  Biol Chem, 389, 1143-1151.  
18278055 A.R.Kusmierczyk, M.J.Kunjappu, M.Funakoshi, and M.Hochstrasser (2008).
A multimeric assembly factor controls the formation of alternative 20S proteasomes.
  Nat Struct Mol Biol, 15, 237-244.  
18644121 A.U.Chouduri, T.Tokumoto, H.Dohra, T.Ushimaru, and S.Yamada (2008).
Functional and biochemical characterization of the 20S proteasome in a yeast temperature-sensitive mutant, rpt6-1.
  BMC Biochem, 9, 20.  
18174173 C.Lipson, G.Alalouf, M.Bajorek, E.Rabinovich, A.Atir-Lande, M.Glickman, and S.Bar-Nun (2008).
A proteasomal ATPase contributes to dislocation of endoplasmic reticulum-associated degradation (ERAD) substrates.
  J Biol Chem, 283, 7166-7175.  
18479220 D.Chen, and Q.P.Dou (2008).
New uses for old copper-binding drugs: converting the pro-angiogenic copper to a specific cancer cell death inducer.
  Expert Opin Ther Targets, 12, 739-748.  
17951257 E.Kario, B.Tirosh, H.L.Ploegh, and A.Navon (2008).
N-linked glycosylation does not impair proteasomal degradation but affects class I major histocompatibility complex presentation.
  J Biol Chem, 283, 244-254.  
18838376 E.Park, J.W.Lee, S.H.Eom, J.H.Seol, and C.H.Chung (2008).
Binding of MG132 or Deletion of the Thr Active Sites in HslV Subunits Increases the Affinity of HslV Protease for HslU ATPase and Makes This Interaction Nucleotide-independent.
  J Biol Chem, 283, 33258-33266.  
18471981 J.Rabl, D.M.Smith, Y.Yu, S.C.Chang, A.L.Goldberg, and Y.Cheng (2008).
Mechanism of gate opening in the 20S proteasome by the proteasomal ATPases.
  Mol Cell, 30, 360-368.
PDB codes: 3c91 3c92
18816064 L.D.Jennings, J.Bohon, M.R.Chance, and S.Licht (2008).
The ClpP N-terminus coordinates substrate access with protease active site reactivity.
  Biochemistry, 47, 11031-11040.  
18519783 L.Wang, S.Kumar, B.L.Fridley, K.R.Kalari, I.Moon, L.L.Pelleymounter, M.A.Hildebrandt, A.Batzler, B.W.Eckloff, E.D.Wieben, and P.R.Greipp (2008).
Proteasome beta subunit pharmacogenomics: gene resequencing and functional genomics.
  Clin Cancer Res, 14, 3503-3513.  
18260085 M.A.Hoyt, S.McDonough, S.A.Pimpl, H.Scheel, K.Hofmann, and P.Coffino (2008).
A genetic screen for Saccharomyces cerevisiae mutants affecting proteasome function, using a ubiquitin-independent substrate.
  Yeast, 25, 199-217.  
  19802337 M.Gaczynska, and P.A.Osmulski (2008).
AFM of biological complexes: what can we learn?
  Curr Opin Colloid Interface Sci, 13, 351-367.  
18163525 M.Verras, P.Gourzi, K.Kalosaka, A.Zacharopoulou, and A.C.Mintzas (2008).
cDNA cloning, characterization, and developmental expression of the 20S proteasome alpha5 subunit in the Mediterranean fruit fly Ceratitis capitata.
  Arch Insect Biochem Physiol, 67, 120-129.  
18502751 N.Y.Zhang, Z.Tang, and C.W.Liu (2008).
alpha-Synuclein protofibrils inhibit 26 S proteasome-mediated protein degradation: understanding the cytotoxicity of protein protofibrils in neurodegenerative disease pathogenesis.
  J Biol Chem, 283, 20288-20298.  
18534977 P.C.da Fonseca, and E.P.Morris (2008).
Structure of the Human 26S Proteasome: SUBUNIT RADIAL DISPLACEMENTS OPEN THE GATE INTO THE PROTEOLYTIC CORE.
  J Biol Chem, 283, 23305-23314.  
18319735 R.Rosenzweig, and M.H.Glickman (2008).
Forging a proteasome alpha-ring with dedicated proteasome chaperones.
  Nat Struct Mol Biol, 15, 218-220.  
18511945 R.Rosenzweig, P.A.Osmulski, M.Gaczynska, and M.H.Glickman (2008).
The central unit within the 19S regulatory particle of the proteasome.
  Nat Struct Mol Biol, 15, 573-580.  
17880010 S.Meiners, A.Ludwig, V.Stangl, and K.Stangl (2008).
Proteasome inhibitors: poisons and remedies.
  Med Res Rev, 28, 309-327.  
17553803 A.A.Horwitz, A.Navon, M.Groll, D.M.Smith, C.Reis, and A.L.Goldberg (2007).
ATP-induced structural transitions in PAN, the proteasome-regulatory ATPase complex in Archaea.
  J Biol Chem, 282, 22921-22929.  
17429695 A.Szabó, M.Pál, P.Deák, P.Kiss, Z.Ujfaludi, T.Pankotai, Z.Lipinszki, and A.Udvardy (2007).
Molecular characterization of the Rpt1/p48B ATPase subunit of the Drosophila melanogaster 26S proteasome.
  Mol Genet Genomics, 278, 17-29.  
17803938 D.M.Smith, S.C.Chang, S.Park, D.Finley, Y.Cheng, and A.L.Goldberg (2007).
Docking of the proteasomal ATPases' carboxyl termini in the 20S proteasome's alpha ring opens the gate for substrate entry.
  Mol Cell, 27, 731-744.  
17327906 H.Seo, K.C.Sonntag, W.Kim, E.Cattaneo, and O.Isacson (2007).
Proteasome activator enhances survival of huntington's disease neuronal model cells.
  PLoS ONE, 2, e238.  
17411433 J.B.Pereira-Leal, E.D.Levy, C.Kamp, and S.A.Teichmann (2007).
Evolution of protein complexes by duplication of homomeric interactions.
  Genome Biol, 8, R51.  
17418826 J.Hanna, and D.Finley (2007).
A proteasome for all occasions.
  FEBS Lett, 581, 2854-2861.  
17455294 J.M.Hunter, M.Lesort, and G.V.Johnson (2007).
Ubiquitin-proteasome system alterations in a striatal cell model of Huntington's disease.
  J Neurosci Res, 85, 1774-1788.  
17696779 L.Borissenko, and M.Groll (2007).
Diversity of proteasomal missions: fine tuning of the immune response.
  Biol Chem, 388, 947-955.  
18026118 M.F.Kleijnen, J.Roelofs, S.Park, N.A.Hathaway, M.Glickman, R.W.King, and D.Finley (2007).
Stability of the proteasome can be regulated allosterically through engagement of its proteolytic active sites.
  Nat Struct Mol Biol, 14, 1180-1188.  
17518699 M.Katsiki, N.Chondrogianni, I.Chinou, A.J.Rivett, and E.S.Gonos (2007).
The olive constituent oleuropein exhibits proteasome stimulatory properties in vitro and confers life span extension of human embryonic fibroblasts.
  Rejuvenation Res, 10, 157-172.  
17466621 M.Kristiansen, P.Deriziotis, D.E.Dimcheff, G.S.Jackson, H.Ovaa, H.Naumann, A.R.Clarke, F.W.van Leeuwen, V.Menéndez-Benito, N.P.Dantuma, J.L.Portis, J.Collinge, and S.J.Tabrizi (2007).
Disease-associated prion protein oligomers inhibit the 26S proteasome.
  Mol Cell, 26, 175-188.  
17143051 R.M.Vabulas (2007).
Proteasome function and protein biosynthesis.
  Curr Opin Clin Nutr Metab Care, 10, 24-31.  
17238925 S.C.Lee, and B.D.Shaw (2007).
A novel interaction between N-myristoylation and the 26S proteasome during cell morphogenesis.
  Mol Microbiol, 63, 1039-1053.  
17889660 Y.Saeki, and K.Tanaka (2007).
Unlocking the proteasome door.
  Mol Cell, 27, 865-867.  
16619030 A.K.Moorthy, O.V.Savinova, J.Q.Ho, V.Y.Wang, D.Vu, and G.Ghosh (2006).
The 20S proteasome processes NF-kappaB1 p105 into p50 in a translation-independent manner.
  EMBO J, 25, 1945-1956.  
16468986 G.Hu, G.Lin, M.Wang, L.Dick, R.M.Xu, C.Nathan, and H.Li (2006).
Structure of the Mycobacterium tuberculosis proteasome and mechanism of inhibition by a peptidyl boronate.
  Mol Microbiol, 59, 1417-1428.
PDB codes: 2fhg 2fhh
16468985 G.Lin, G.Hu, C.Tsu, Y.Z.Kunes, H.Li, L.Dick, T.Parsons, P.Li, Z.Chen, P.Zwickl, N.Weich, and C.Nathan (2006).
Mycobacterium tuberculosis prcBA genes encode a gated proteasome with broad oligopeptide specificity.
  Mol Microbiol, 59, 1405-1416.  
16858705 K.Schulze, A.Mulder, A.Tinazli, and R.Tampé (2006).
Controlling the activity of the 20S proteasome complex by synthetic gatekeepers.
  Angew Chem Int Ed Engl, 45, 5702-5705.  
16886005 L.Tian, and A.Matouschek (2006).
Where to start and when to stop.
  Nat Struct Mol Biol, 13, 668-670.  
16648584 P.J.Neuburger, K.J.Saville, J.Zeng, K.A.Smyth, and J.M.Belote (2006).
A genetic suppressor of two dominant temperature-sensitive lethal proteasome mutants of Drosophila melanogaster is itself a mutated proteasome subunit gene.
  Genetics, 173, 1377-1387.  
16793767 S.Yamada, J.Niwa, S.Ishigaki, M.Takahashi, T.Ito, J.Sone, M.Doyu, and G.Sobue (2006).
Archaeal proteasomes effectively degrade aggregation-prone proteins and reduce cellular toxicities in mammalian cells.
  J Biol Chem, 281, 23842-23851.  
16487055 T.C.Squier (2006).
Redox modulation of cellular metabolism through targeted degradation of signaling proteins by the proteasome.
  Antioxid Redox Signal, 8, 217-228.  
16987959 T.Shibatani, E.J.Carlson, F.Larabee, A.L.McCormack, K.Früh, and W.R.Skach (2006).
Global organization and function of mammalian cytosolic proteasome pools: Implications for PA28 and 19S regulatory complexes.
  Mol Biol Cell, 17, 4962-4971.  
16877706 T.V.Rotanova, I.Botos, E.E.Melnikov, F.Rasulova, A.Gustchina, M.R.Maurizi, and A.Wlodawer (2006).
Slicing a protease: structural features of the ATP-dependent Lon proteases gleaned from investigations of isolated domains.
  Protein Sci, 15, 1815-1828.  
15701650 A.Gribun, M.S.Kimber, R.Ching, R.Sprangers, K.M.Fiebig, and W.A.Houry (2005).
The ClpP double ring tetradecameric protease exhibits plastic ring-ring interactions, and the N termini of its subunits form flexible loops that are essential for ClpXP and ClpAP complex formation.
  J Biol Chem, 280, 16185-16196.
PDB code: 1y7o
16181324 B.Strehl, U.Seifert, E.Krüger, S.Heink, U.Kuckelkorn, and P.M.Kloetzel (2005).
Interferon-gamma, the functional plasticity of the ubiquitin-proteasome system, and MHC class I antigen processing.
  Immunol Rev, 207, 19-30.  
16337593 D.M.Smith, G.Kafri, Y.Cheng, D.Ng, T.Walz, and A.L.Goldberg (2005).
ATP binding to PAN or the 26S ATPases causes association with the 20S proteasome, gate opening, and translocation of unfolded proteins.
  Mol Cell, 20, 687-698.  
15611133 E.Isono, N.Saito, N.Kamata, Y.Saeki, and A.Toh-E (2005).
Functional analysis of Rpn6p, a lid component of the 26 S proteasome, using temperature-sensitive rpn6 mutants of the yeast Saccharomyces cerevisiae.
  J Biol Chem, 280, 6537-6547.  
15948901 G.A.Roth, B.Moser, C.Krenn, F.Roth-Walter, H.Hetz, S.Richter, M.Brunner, E.Jensen-Jarolim, E.Wolner, K.Hoetzenecker, G.Boltz-Nitulescu, and H.J.Ankersmit (2005).
Heightened levels of circulating 20S proteasome in critically ill patients.
  Eur J Clin Invest, 35, 399-403.  
15678420 M.Groll, M.Bochtler, H.Brandstetter, T.Clausen, and R.Huber (2005).
Molecular machines for protein degradation.
  Chembiochem, 6, 222-256.  
15653075 M.Rechsteiner, and C.P.Hill (2005).
Mobilizing the proteolytic machine: cell biological roles of proteasome activators and inhibitors.
  Trends Cell Biol, 15, 27-33.  
16201867 M.Schmidt, J.Hanna, S.Elsasser, and D.Finley (2005).
Proteasome-associated proteins: regulation of a proteolytic machine.
  Biol Chem, 386, 725-737.  
15778719 M.Schmidt, W.Haas, B.Crosas, P.G.Santamaria, S.P.Gygi, T.Walz, and D.Finley (2005).
The HEAT repeat protein Blm10 regulates the yeast proteasome by capping the core particle.
  Nat Struct Mol Biol, 12, 294-303.  
16337594 P.Sdek, H.Ying, D.L.Chang, W.Qiu, H.Zheng, R.Touitou, M.J.Allday, and Z.X.Xiao (2005).
MDM2 promotes proteasome-dependent ubiquitin-independent degradation of retinoblastoma protein.
  Mol Cell, 20, 699-708.  
15780906 R.Farràs, G.Bossis, E.Andermarcher, I.Jariel-Encontre, and M.Piechaczyk (2005).
Mechanisms of delivery of ubiquitylated proteins to the proteasome: new target for anti-cancer therapy?
  Crit Rev Oncol Hematol, 54, 31-51.  
16115876 S.G.Kang, M.N.Dimitrova, J.Ortega, A.Ginsburg, and M.R.Maurizi (2005).
Human mitochondrial ClpP is a stable heptamer that assembles into a tetradecamer in the presence of ClpX.
  J Biol Chem, 280, 35424-35432.  
15831487 Y.Park, Y.P.Hwang, J.S.Lee, S.H.Seo, S.K.Yoon, and J.B.Yoon (2005).
Proteasomal ATPase-associated factor 1 negatively regulates proteasome activity by interacting with proteasomal ATPases.
  Mol Cell Biol, 25, 3842-3853.  
14581483 A.Guterman, and M.H.Glickman (2004).
Complementary roles for Rpn11 and Ubp6 in deubiquitination and proteolysis by the proteasome.
  J Biol Chem, 279, 1729-1738.  
15066131 B.Xu, B.Monsarrat, J.E.Gairin, and E.Girbal-Neuhauser (2004).
Effect of ajoene, a natural antitumor small molecule, on human 20S proteasome activity in vitro and in human leukemic HL60 cells.
  Fundam Clin Pharmacol, 18, 171-180.  
15039430 D.M.Janse, B.Crosas, D.Finley, and G.M.Church (2004).
Localization to the proteasome is sufficient for degradation.
  J Biol Chem, 279, 21415-21420.  
15102831 E.Isono, Y.Saeki, H.Yokosawa, and A.Toh-e (2004).
Rpn7 Is required for the structural integrity of the 26 S proteasome of Saccharomyces cerevisiae.
  J Biol Chem, 279, 27168-27176.  
14739934 I.Velichutina, P.L.Connerly, C.S.Arendt, X.Li, and M.Hochstrasser (2004).
Plasticity in eucaryotic 20S proteasome ring assembly revealed by a subunit deletion in yeast.
  EMBO J, 23, 500-510.  
15319444 J.E.Whittier, Y.Xiong, M.C.Rechsteiner, and T.C.Squier (2004).
Hsp90 enhances degradation of oxidized calmodulin by the 20 S proteasome.
  J Biol Chem, 279, 46135-46142.  
15377232 J.Smalle, and R.D.Vierstra (2004).
The ubiquitin 26S proteasome proteolytic pathway.
  Annu Rev Plant Biol, 55, 555-590.  
15368577 M.Kaiser, M.Groll, C.Siciliano, I.Assfalg-Machleidt, E.Weyher, J.Kohno, A.G.Milbradt, C.Renner, R.Huber, and L.Moroder (2004).
Binding mode of TMC-95A analogues to eukaryotic 20S proteasome.
  Chembiochem, 5, 1256-1266.  
15224091 P.M.Kloetzel (2004).
Generation of major histocompatibility complex class I antigens: functional interplay between proteasomes and TPPII.
  Nat Immunol, 5, 661-669.  
15068806 P.Venkatraman, R.Wetzel, M.Tanaka, N.Nukina, and A.L.Goldberg (2004).
Eukaryotic proteasomes cannot digest polyglutamine sequences and release them during degradation of polyglutamine-containing proteins.
  Mol Cell, 14, 95.  
14623884 P.Yang, H.Fu, J.Walker, C.M.Papa, J.Smalle, Y.M.Ju, and R.D.Vierstra (2004).
Purification of the Arabidopsis 26 S proteasome: biochemical and molecular analyses revealed the presence of multiple isoforms.
  J Biol Chem, 279, 6401-6413.  
15209385 R.Hartmann-Petersen, and C.Gordon (2004).
Integral UBL domain proteins: a family of proteasome interacting proteins.
  Semin Cell Dev Biol, 15, 247-259.  
15064753 S.A.Joshi, G.L.Hersch, T.A.Baker, and R.T.Sauer (2004).
Communication between ClpX and ClpP during substrate processing and degradation.
  Nat Struct Mol Biol, 11, 404-411.  
15175655 S.Hutschenreiter, A.Tinazli, K.Model, and R.Tampé (2004).
Two-substrate association with the 20S proteasome at single-molecule level.
  EMBO J, 23, 2488-2497.  
15311270 S.Prakash, L.Tian, K.S.Ratliff, R.E.Lehotzky, and A.Matouschek (2004).
An unstructured initiation site is required for efficient proteasome-mediated degradation.
  Nat Struct Mol Biol, 11, 830-837.  
15117943 T.Sone, Y.Saeki, A.Toh-e, and H.Yokosawa (2004).
Sem1p is a novel subunit of the 26 S proteasome from Saccharomyces cerevisiae.
  J Biol Chem, 279, 28807-28816.  
12941688 A.Förster, F.G.Whitby, and C.P.Hill (2003).
The pore of activated 20S proteasomes has an ordered 7-fold symmetric conformation.
  EMBO J, 22, 4356-4364.  
12815064 A.F.Kisselev, M.Garcia-Calvo, H.S.Overkleeft, E.Peterson, M.W.Pennington, H.L.Ploegh, N.A.Thornberry, and A.L.Goldberg (2003).
The caspase-like sites of proteasomes, their substrate specificity, new inhibitors and substrates, and allosteric interactions with the trypsin-like sites.
  J Biol Chem, 278, 35869-35877.  
14685250 A.L.Goldberg (2003).
Protein degradation and protection against misfolded or damaged proteins.
  Nature, 426, 895-899.  
12581666 A.Matouschek (2003).
Protein unfolding--an important process in vivo?
  Curr Opin Struct Biol, 13, 98.  
12606569 C.Hirsch, D.Blom, and H.L.Ploegh (2003).
A role for N-glycanase in the cytosolic turnover of glycoproteins.
  EMBO J, 22, 1036-1046.  
12481023 C.W.Liu, M.J.Corboy, G.N.DeMartino, and P.J.Thomas (2003).
Endoproteolytic activity of the proteasome.
  Science, 299, 408-411.  
12948749 J.A.Maupin-Furlow, S.J.Kaczowka, C.J.Reuter, K.Zuobi-Hasona, and M.A.Gil (2003).
Archaeal proteasomes: potential in metabolic engineering.
  Metab Eng, 5, 151-163.  
12842014 M.Bajorek, D.Finley, and M.H.Glickman (2003).
Proteasome disassembly and downregulation is correlated with viability during stationary phase.
  Curr Biol, 13, 1140-1144.  
12672453 M.Groll, and R.Huber (2003).
Substrate access and processing by the 20S proteasome core particle.
  Int J Biochem Cell Biol, 35, 606-616.  
14675543 M.Groll, and T.Clausen (2003).
Molecular shredders: how proteasomes fulfill their role.
  Curr Opin Struct Biol, 13, 665-673.  
14522244 M.Mishto, A.Santoro, E.Bellavista, M.Bonafé, D.Monti, and C.Franceschi (2003).
Immunoproteasomes and immunosenescence.
  Ageing Res Rev, 2, 419-432.  
12486135 P.G.Santamaria, D.Finley, J.P.Ballesta, and M.Remacha (2003).
Rpn6p, a proteasome subunit from Saccharomyces cerevisiae, is essential for the assembly and activity of the 26 S proteasome.
  J Biol Chem, 278, 6687-6695.  
12517449 R.Hartmann-Petersen, M.Seeger, and C.Gordon (2003).
Transferring substrates to the 26S proteasome.
  Trends Biochem Sci, 28, 26-31.  
12674498 R.Stohwasser, H.G.Holzhütter, U.Lehmann, P.Henklein, and P.M.Kloetzel (2003).
Hepatitis B virus HBx peptide 116-138 and proteasome activator PA28 compete for binding to the proteasome alpha4/MC6 subunit.
  Biol Chem, 384, 39-49.  
12676932 S.Meiners, D.Heyken, A.Weller, A.Ludwig, K.Stangl, P.M.Kloetzel, and E.Krüger (2003).
Inhibition of proteasome activity induces concerted expression of proteasome genes and de novo formation of Mammalian proteasomes.
  J Biol Chem, 278, 21517-21525.  
12743025 Z.Kostova, and D.H.Wolf (2003).
For whom the bell tolls: protein quality control of the endoplasmic reticulum and the ubiquitin-proteasome connection.
  EMBO J, 22, 2309-2317.  
12377129 A.E.Todd, C.A.Orengo, and J.M.Thornton (2002).
Sequence and structural differences between enzyme and nonenzyme homologs.
  Structure, 10, 1435-1451.  
11927581 A.F.Kisselev, D.Kaganovich, and A.L.Goldberg (2002).
Binding of hydrophobic peptides to several non-catalytic sites promotes peptide hydrolysis by all active sites of 20 S proteasomes. Evidence for peptide-induced channel opening in the alpha-rings.
  J Biol Chem, 277, 22260-22270.  
12270919 A.V.Kajava (2002).
What curves alpha-solenoids? Evidence for an alpha-helical toroid structure of Rpn1 and Rpn2 proteins of the 26 S proteasome.
  J Biol Chem, 277, 49791-49798.  
12080075 C.Lee, S.Prakash, and A.Matouschek (2002).
Concurrent translocation of multiple polypeptide chains through the proteasomal degradation channel.
  J Biol Chem, 277, 34760-34765.  
11739392 C.Wójcik, and G.N.DeMartino (2002).
Analysis of Drosophila 26 S proteasome using RNA interference.
  J Biol Chem, 277, 6188-6197.  
11988752 D.Finley (2002).
Ubiquitin chained and crosslinked.
  Nat Cell Biol, 4, E121-E123.  
12200039 G.Carrard, A.L.Bulteau, I.Petropoulos, and B.Friguet (2002).
Impairment of proteasome structure and function in aging.
  Int J Biochem Cell Biol, 34, 1461-1474.  
  12399382 H.B.McDonald, A.H.Helfant, E.M.Mahony, S.K.Khosla, and L.Goetsch (2002).
Mutational analysis reveals a role for the C terminus of the proteasome subunit Rpt4p in spindle pole body duplication in Saccharomyces cerevisiae.
  Genetics, 162, 705-720.  
12011053 I.S.Seong, M.S.Kang, M.K.Choi, J.W.Lee, O.J.Koh, J.Wang, S.H.Eom, and C.H.Chung (2002).
The C-terminal tails of HslU ATPase act as a molecular switch for activation of HslV peptidase.
  J Biol Chem, 277, 25976-25982.  
12234933 J.Ortega, H.S.Lee, M.R.Maurizi, and A.C.Steven (2002).
Alternating translocation of protein substrates from both ends of ClpXP protease.
  EMBO J, 21, 4938-4949.  
  12488589 K.Sweder, and K.Madura (2002).
Regulation of repair by the 26S proteasome.
  J Biomed Biotechnol, 2, 94.  
11988749 M.Rape, and S.Jentsch (2002).
Taking a bite: proteasomal protein processing.
  Nat Cell Biol, 4, E113-E116.  
12033938 P.A.Osmulski, and M.Gaczynska (2002).
Nanoenzymology of the 20S proteasome: proteasomal actions are controlled by the allosteric transition.
  Biochemistry, 41, 7047-7053.  
12032076 P.Cascio, M.Call, B.M.Petre, T.Walz, and A.L.Goldberg (2002).
Properties of the hybrid form of the 26S proteasome containing both 19S and PA28 complexes.
  EMBO J, 21, 2636-2645.  
12032294 R.Ramachandran, C.Hartmann, H.K.Song, R.Huber, and M.Bochtler (2002).
Functional interactions of HslV (ClpQ) with the ATPase HslU (ClpY).
  Proc Natl Acad Sci U S A, 99, 7396-7401.  
12183636 R.Verma, L.Aravind, R.Oania, W.H.McDonald, J.R.Yates, E.V.Koonin, and R.J.Deshaies (2002).
Role of Rpn11 metalloprotease in deubiquitination and degradation by the 26S proteasome.
  Science, 298, 611-615.  
11956289 U.Kuckelkorn, T.Ruppert, B.Strehl, P.R.Jungblut, U.Zimny-Arndt, S.Lamer, I.Prinz, I.Drung, P.M.Kloetzel, S.H.Kaufmann, and U.Steinhoff (2002).
Link between organ-specific antigen processing by 20S proteasomes and CD8(+) T cell-mediated autoimmunity.
  J Exp Med, 195, 983-990.  
  12370088 V.Maytal-Kivity, N.Reis, K.Hofmann, and M.H.Glickman (2002).
MPN+, a putative catalytic motif found in a subset of MPN domain proteins from eukaryotes and prokaryotes, is critical for Rpn11 function.
  BMC Biochem, 3, 28.  
11840541 Y.Iwafune, H.Kawasaki, and H.Hirano (2002).
Electrophoretic analysis of phosphorylation of the yeast 20S proteasome.
  Electrophoresis, 23, 329-338.  
12502737 Y.Tone, and A.Toh-E (2002).
Nob1p is required for biogenesis of the 26S proteasome and degraded upon its maturation in Saccharomyces cerevisiae.
  Genes Dev, 16, 3142-3157.  
11854272 Z.Li, C.B.Zou, Y.Yao, M.A.Hoyt, S.McDonough, Z.B.Mackey, P.Coffino, and C.C.Wang (2002).
An easily dissociated 26 S proteasome catalyzes an essential ubiquitin-mediated protein degradation pathway in Trypanosoma brucei.
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11514224 A.F.Kisselev, and A.L.Goldberg (2001).
Proteasome inhibitors: from research tools to drug candidates.
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11779508 A.Navon, and A.L.Goldberg (2001).
Proteins are unfolded on the surface of the ATPase ring before transport into the proteasome.
  Mol Cell, 8, 1339-1349.  
11473704 C.Ingvardsen, and B.Veierskov (2001).
Ubiquitin- and proteasome-dependent proteolysis in plants.
  Physiol Plant, 112, 451-459.  
11295500 J.Li, and M.Rechsteiner (2001).
Molecular dissection of the 11S REG (PA28) proteasome activators.
  Biochimie, 83, 373-383.  
11410931 J.Myung, K.B.Kim, and C.M.Crews (2001).
The ubiquitin-proteasome pathway and proteasome inhibitors.
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12540272 M.Hofmann, A.K.Nussbaum, N.P.Emmerich, L.Stoltze, and H.Schild (2001).
Mechanisms of MHC class I-restricted antigen presentation.
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11295491 N.Benaroudj, E.Tarcsa, P.Cascio, and A.L.Goldberg (2001).
The unfolding of substrates and ubiquitin-independent protein degradation by proteasomes.
  Biochimie, 83, 311-318.  
11387208 R.Farrás, A.Ferrando, J.Jásik, T.Kleinow, L.Okrész, A.Tiburcio, K.Salchert, C.del Pozo, J.Schell, and C.Koncz (2001).
SKP1-SnRK protein kinase interactions mediate proteasomal binding of a plant SCF ubiquitin ligase.
  EMBO J, 20, 2742-2756.  
11500370 S.Jäger, J.Strayle, W.Heinemeyer, and D.H.Wolf (2001).
Cic1, an adaptor protein specifically linking the 26S proteasome to its substrate, the SCF component Cdc4.
  EMBO J, 20, 4423-4431.  
11590019 S.J.Russell, F.Gonzalez, L.Joshua-Tor, and S.A.Johnston (2001).
Selective chemical inactivation of AAA proteins reveals distinct functions of proteasomal ATPases.
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11390439 W.Chen, C.C.Norbury, Y.Cho, J.W.Yewdell, and J.R.Bennink (2001).
Immunoproteasomes shape immunodominance hierarchies of antiviral CD8(+) T cells at the levels of T cell repertoire and presentation of viral antigens.
  J Exp Med, 193, 1319-1326.  
11114186 H.K.Song, C.Hartmann, R.Ramachandran, M.Bochtler, R.Behrendt, L.Moroder, and R.Huber (2000).
Mutational studies on HslU and its docking mode with HslV.
  Proc Natl Acad Sci U S A, 97, 14103-14108.
PDB code: 1e94
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.

 

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