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Contents |
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* Residue conservation analysis
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PDB id:
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DNA binding protein
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Title:
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A crystal structure of the rad51 filament
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Structure:
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DNA repair protein rad51. Chain: a, b, c, d, e, f. Fragment: del(1-79). Engineered: yes
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Source:
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Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Gene: rad51, yer095w. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Biol. unit:
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Dimer (from PDB file)
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Resolution:
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3.25Å
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R-factor:
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0.273
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R-free:
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0.320
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Authors:
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A.B.Conway,T.W.Lynch,Y.Zhang,G.S.Fortin,L.S.Symington,P.A.Rice
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Key ref:
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A.B.Conway
et al.
(2004).
Crystal structure of a Rad51 filament.
Nat Struct Mol Biol,
11,
791-796.
PubMed id:
DOI:
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Date:
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06-Apr-04
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Release date:
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13-Jul-04
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PROCHECK
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Headers
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References
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DOI no:
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Nat Struct Mol Biol
11:791-796
(2004)
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PubMed id:
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Crystal structure of a Rad51 filament.
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A.B.Conway,
T.W.Lynch,
Y.Zhang,
G.S.Fortin,
C.W.Fung,
L.S.Symington,
P.A.Rice.
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ABSTRACT
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Rad51, the major eukaryotic homologous recombinase, is important for the repair
of DNA damage and the maintenance of genomic diversity and stability. The active
form of this DNA-dependent ATPase is a helical filament within which the search
for homology and strand exchange occurs. Here we present the crystal structure
of a Saccharomyces cerevisiae Rad51 filament formed by a gain-of-function
mutant. This filament has a longer pitch than that seen in crystals of Rad51's
prokaryotic homolog RecA, and places the ATPase site directly at a new interface
between protomers. Although the filament exhibits approximate six-fold symmetry,
alternate protein-protein interfaces are slightly different, implying that the
functional unit of Rad51 within the filament may be a dimer. Additionally, we
show that mutation of His352, which lies at this new interface, markedly
disrupts DNA binding.
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Selected figure(s)
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Figure 2.
Figure 2. Filaments of Rad51 and RecA. (a) The Rad51 filament
found in these crystals has a helical pitch of 130 Å and is
composed of two crystallographically independent monomers
(yellow and green) that alternate to form a filament with exact
three-fold but only approximate six-fold screw symmetry. A
sulfate (black spheres) mimics the binding of phosphate in the
ATPase site, which is nestled directly at the interface between
two protomers (arrow). One of the N-terminal domains that line
the upper surface of the filament is circled. (b) The filament
formed in RecA crystals has a helical pitch of  83
Å and is shown with each crystallographically equivalent monomer
colored differently
(,
).
The structurally conserved ATPase
domains are in the same orientation relative to the filament
axis as in a. The crystallographically observed ADP is in
ball-and-stick form, positioned a substantial distance from the
adjacent protomer. The C-terminal domains (circled) line the
lower surface of the filament.
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Figure 3.
Figure 3. Oligomerization of Rad51. (a) The Rad51 filament
assembles by packing a  -strand
from the interdomain linker of one protomer (green) onto the
central sheet of the adjacent monomer (yellow). Interactions
between ATPase domains include a helix (purple) that is
disordered in nonfilament structures of RadA and Rad51. (b) A
peptide from BRCA2 (orange) bound to the human Rad51 ATPase
domain (yellow)
().
The peptide mimics the -strand
interaction motif of intact Rad51. The loop following the
disordered helix is purple.
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The above figures are
reprinted
by permission from Macmillan Publishers Ltd:
Nat Struct Mol Biol
(2004,
11,
791-796)
copyright 2004.
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Figures were
selected
by the author.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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D.Ristic,
R.Kanaar,
and
C.Wyman
(2011).
Visualizing RAD51-mediated joint molecules: implications for recombination mechanism and the effect of sequence heterology.
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Nucleic Acids Res,
39,
155-167.
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|
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|
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A.L.Okorokov,
Y.L.Chaban,
D.V.Bugreev,
J.Hodgkinson,
A.V.Mazin,
and
E.V.Orlova
(2010).
Structure of the hDmc1-ssDNA filament reveals the principles of its architecture.
|
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PLoS One,
5,
e8586.
|
|
|
|
|
|
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E.Rajendra,
and
A.R.Venkitaraman
(2010).
Two modules in the BRC repeats of BRCA2 mediate structural and functional interactions with the RAD51 recombinase.
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Nucleic Acids Res,
38,
82-96.
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|
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J.Chen,
N.Villanueva,
M.A.Rould,
and
S.W.Morrical
(2010).
Insights into the mechanism of Rad51 recombinase from the structure and properties of a filament interface mutant.
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Nucleic Acids Res,
38,
4889-4906.
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PDB code:
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J.Liu,
and
S.W.Morrical
(2010).
Assembly and dynamics of the bacteriophage T4 homologous recombination machinery.
|
| |
Virol J,
7,
357.
|
|
|
|
|
|
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V.Marini,
and
L.Krejci
(2010).
Srs2: the "Odd-Job Man" in DNA repair.
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DNA Repair (Amst),
9,
268-275.
|
|
|
|
|
|
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Y.Takizawa,
Y.Qing,
M.Takaku,
T.Ishida,
Y.Morozumi,
T.Tsujita,
T.Kogame,
K.Hirota,
M.Takahashi,
T.Shibata,
H.Kurumizaka,
and
S.Takeda
(2010).
GEMIN2 promotes accumulation of RAD51 at double-strand breaks in homologous recombination.
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Nucleic Acids Res,
38,
5059-5074.
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|
|
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|
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A.A.Grigorescu,
J.H.Vissers,
D.Ristic,
Y.Z.Pigli,
T.W.Lynch,
C.Wyman,
and
P.A.Rice
(2009).
Inter-subunit interactions that coordinate Rad51's activities.
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Nucleic Acids Res,
37,
557-567.
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|
|
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|
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A.Reymer,
K.Frykholm,
K.Morimatsu,
M.Takahashi,
and
B.Nordén
(2009).
Structure of human Rad51 protein filament from molecular modeling and site-specific linear dichroism spectroscopy.
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Proc Natl Acad Sci U S A,
106,
13248-13253.
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|
|
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C.Seong,
S.Colavito,
Y.Kwon,
P.Sung,
and
L.Krejci
(2009).
Regulation of Rad51 recombinase presynaptic filament assembly via interactions with the Rad52 mediator and the Srs2 anti-recombinase.
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J Biol Chem,
284,
24363-24371.
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D.Lucarelli,
Y.A.Wang,
V.E.Galkin,
X.Yu,
D.B.Wigley,
and
E.H.Egelman
(2009).
The RecB nuclease domain binds to RecA-DNA filaments: implications for filament loading.
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J Mol Biol,
391,
269-274.
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E.Antony,
E.J.Tomko,
Q.Xiao,
L.Krejci,
T.M.Lohman,
and
T.Ellenberger
(2009).
Srs2 disassembles Rad51 filaments by a protein-protein interaction triggering ATP turnover and dissociation of Rad51 from DNA.
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Mol Cell,
35,
105-115.
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H.Arata,
A.Dupont,
J.Miné-Hattab,
L.Disseau,
A.Renodon-Cornière,
M.Takahashi,
J.L.Viovy,
and
G.Cappello
(2009).
Direct observation of twisting steps during Rad51 polymerization on DNA.
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| |
Proc Natl Acad Sci U S A,
106,
19239-19244.
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|
|
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J.Hikiba,
Y.Takizawa,
S.Ikawa,
T.Shibata,
and
H.Kurumizaka
(2009).
Biochemical analysis of the human DMC1-I37N polymorphism.
|
| |
FEBS J,
276,
457-465.
|
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|
|
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J.Hilario,
I.Amitani,
R.J.Baskin,
and
S.C.Kowalczykowski
(2009).
Direct imaging of human Rad51 nucleoprotein dynamics on individual DNA molecules.
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Proc Natl Acad Sci U S A,
106,
361-368.
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J.N.Farb,
and
S.W.Morrical
(2009).
Role of allosteric switch residue histidine 195 in maintaining active-site asymmetry in presynaptic filaments of bacteriophage T4 UvsX recombinase.
|
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J Mol Biol,
385,
393-404.
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M.Budzowska,
and
R.Kanaar
(2009).
Mechanisms of dealing with DNA damage-induced replication problems.
|
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Cell Biochem Biophys,
53,
17-31.
|
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|
|
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|
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M.Sinha,
and
C.L.Peterson
(2009).
Chromatin dynamics during repair of chromosomal DNA double-strand breaks.
|
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Epigenomics,
1,
371-385.
|
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|
|
|
|
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X.P.Zhang,
V.E.Galkin,
X.Yu,
E.H.Egelman,
and
W.D.Heyer
(2009).
Loop 2 in Saccharomyces cerevisiae Rad51 protein regulates filament formation and ATPase activity.
|
| |
Nucleic Acids Res,
37,
158-171.
|
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|
|
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|
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Y.Morozumi,
Y.Takizawa,
M.Takaku,
and
H.Kurumizaka
(2009).
Human PSF binds to RAD51 and modulates its homologous-pairing and strand-exchange activities.
|
| |
Nucleic Acids Res,
37,
4296-4307.
|
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|
|
|
|
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Y.W.Chang,
T.P.Ko,
C.D.Lee,
Y.C.Chang,
K.A.Lin,
C.S.Chang,
A.H.Wang,
and
T.F.Wang
(2009).
Three new structures of left-handed RADA helical filaments: structural flexibility of N-terminal domain is critical for recombinase activity.
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PLoS ONE,
4,
e4890.
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PDB codes:
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C.Rajanikant,
M.Melzer,
B.J.Rao,
and
J.K.Sainis
(2008).
Homologous recombination properties of OsRad51, a recombinase from rice.
|
| |
Plant Mol Biol,
68,
479-491.
|
|
|
|
|
|
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J.Hikiba,
K.Hirota,
W.Kagawa,
S.Ikawa,
T.Kinebuchi,
I.Sakane,
Y.Takizawa,
S.Yokoyama,
B.Mandon-Pépin,
A.Nicolas,
T.Shibata,
K.Ohta,
and
H.Kurumizaka
(2008).
Structural and functional analyses of the DMC1-M200V polymorphism found in the human population.
|
| |
Nucleic Acids Res,
36,
4181-4190.
|
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PDB code:
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J.M.Cox,
H.Li,
E.A.Wood,
S.Chitteni-Pattu,
R.B.Inman,
and
M.M.Cox
(2008).
Defective Dissociation of a "Slow" RecA Mutant Protein Imparts an Escherichia coli Growth Defect.
|
| |
J Biol Chem,
283,
24909-24921.
|
|
|
|
|
|
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J.Nomme,
Y.Takizawa,
S.F.Martinez,
A.Renodon-Cornière,
F.Fleury,
P.Weigel,
K.Yamamoto,
H.Kurumizaka,
and
M.Takahashi
(2008).
Inhibition of filament formation of human Rad51 protein by a small peptide derived from the BRC-motif of the BRCA2 protein.
|
| |
Genes Cells,
13,
471-481.
|
|
|
|
|
|
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K.Jayathilaka,
S.D.Sheridan,
T.D.Bold,
K.Bochenska,
H.L.Logan,
R.R.Weichselbaum,
D.K.Bishop,
and
P.P.Connell
(2008).
A chemical compound that stimulates the human homologous recombination protein RAD51.
|
| |
Proc Natl Acad Sci U S A,
105,
15848-15853.
|
|
|
|
|
|
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K.T.Ehmsen,
and
W.D.Heyer
(2008).
Biochemistry of Meiotic Recombination: Formation, Processing, and Resolution of Recombination Intermediates.
|
| |
Genome Dyn Stab,
3,
91.
|
|
|
|
|
|
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M.López-Casamichana,
E.Orozco,
L.A.Marchat,
and
C.López-Camarillo
(2008).
Transcriptional profile of the homologous recombination machinery and characterization of the EhRAD51 recombinase in response to DNA damage in Entamoeba histolytica.
|
| |
BMC Mol Biol,
9,
35.
|
|
|
|
|
|
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N.Mazloum,
Q.Zhou,
and
W.K.Holloman
(2008).
D-loop formation by Brh2 protein of Ustilago maydis.
|
| |
Proc Natl Acad Sci U S A,
105,
524-529.
|
|
|
|
|
|
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P.S.Malik,
and
L.S.Symington
(2008).
Rad51 gain-of-function mutants that exhibit high affinity DNA binding cause DNA damage sensitivity in the absence of Srs2.
|
| |
Nucleic Acids Res,
36,
6504-6510.
|
|
|
|
|
|
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X.Li,
and
W.D.Heyer
(2008).
Homologous recombination in DNA repair and DNA damage tolerance.
|
| |
Cell Res,
18,
99.
|
|
|
|
|
|
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Z.Chen,
H.Yang,
and
N.P.Pavletich
(2008).
Mechanism of homologous recombination from the RecA-ssDNA/dsDNA structures.
|
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Nature,
453,
489-484.
|
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PDB codes:
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A.L.Forget,
M.S.Loftus,
D.A.McGrew,
B.T.Bennett,
and
K.L.Knight
(2007).
The human Rad51 K133A mutant is functional for DNA double-strand break repair in human cells.
|
| |
Biochemistry,
46,
3566-3575.
|
|
|
|
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|
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F.Esashi,
V.E.Galkin,
X.Yu,
E.H.Egelman,
and
S.C.West
(2007).
Stabilization of RAD51 nucleoprotein filaments by the C-terminal region of BRCA2.
|
| |
Nat Struct Mol Biol,
14,
468-474.
|
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|
|
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J.Miné,
L.Disseau,
M.Takahashi,
G.Cappello,
M.Dutreix,
and
J.L.Viovy
(2007).
Real-time measurements of the nucleation, growth and dissociation of single Rad51-DNA nucleoprotein filaments.
|
| |
Nucleic Acids Res,
35,
7171-7187.
|
|
|
|
|
|
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L.T.Chen,
T.P.Ko,
Y.C.Chang,
K.A.Lin,
C.S.Chang,
A.H.Wang,
and
T.F.Wang
(2007).
Crystal structure of the left-handed archaeal RadA helical filament: identification of a functional motif for controlling quaternary structures and enzymatic functions of RecA family proteins.
|
| |
Nucleic Acids Res,
35,
1787-1801.
|
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PDB code:
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L.T.Chen,
T.P.Ko,
Y.W.Chang,
K.A.Lin,
A.H.Wang,
and
T.F.Wang
(2007).
Structural and functional analyses of five conserved positively charged residues in the L1 and N-terminal DNA binding motifs of archaeal RADA protein.
|
| |
PLoS ONE,
2,
e858.
|
|
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PDB code:
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M.A.Abbani,
C.V.Papagiannis,
M.D.Sam,
D.Cascio,
R.C.Johnson,
and
R.T.Clubb
(2007).
Structure of the cooperative Xis-DNA complex reveals a micronucleoprotein filament that regulates phage lambda intasome assembly.
|
| |
Proc Natl Acad Sci U S A,
104,
2109-2114.
|
|
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PDB code:
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|
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M.I.Petalcorin,
V.E.Galkin,
X.Yu,
E.H.Egelman,
and
S.J.Boulton
(2007).
Stabilization of RAD-51-DNA filaments via an interaction domain in Caenorhabditis elegans BRCA2.
|
| |
Proc Natl Acad Sci U S A,
104,
8299-8304.
|
|
|
|
|
|
|
M.Modesti,
D.Ristic,
T.van der Heijden,
C.Dekker,
J.van Mameren,
E.J.Peterman,
G.J.Wuite,
R.Kanaar,
and
C.Wyman
(2007).
Fluorescent human RAD51 reveals multiple nucleation sites and filament segments tightly associated along a single DNA molecule.
|
| |
Structure,
15,
599-609.
|
|
|
|
|
|
|
O.R.Davies,
and
L.Pellegrini
(2007).
Interaction with the BRCA2 C terminus protects RAD51-DNA filaments from disassembly by BRC repeats.
|
| |
Nat Struct Mol Biol,
14,
475-483.
|
|
|
|
|
|
|
R.L.Barnes,
and
R.McCulloch
(2007).
Trypanosoma brucei homologous recombination is dependent on substrate length and homology, though displays a differential dependence on mismatch repair as substrate length decreases.
|
| |
Nucleic Acids Res,
35,
3478-3493.
|
|
|
|
|
|
|
T.Ishida,
Y.Takizawa,
I.Sakane,
and
H.Kurumizaka
(2007).
Altered DNA binding by the human Rad51-R150Q mutant found in breast cancer patients.
|
| |
Biol Pharm Bull,
30,
1374-1378.
|
|
|
|
|
|
|
T.Thorslund,
and
S.C.West
(2007).
BRCA2: a universal recombinase regulator.
|
| |
Oncogene,
26,
7720-7730.
|
|
|
|
|
|
|
T.van der Heijden,
R.Seidel,
M.Modesti,
R.Kanaar,
C.Wyman,
and
C.Dekker
(2007).
Real-time assembly and disassembly of human RAD51 filaments on individual DNA molecules.
|
| |
Nucleic Acids Res,
35,
5646-5657.
|
|
|
|
|
|
|
A.Granéli,
C.C.Yeykal,
R.B.Robertson,
and
E.C.Greene
(2006).
Long-distance lateral diffusion of human Rad51 on double-stranded DNA.
|
| |
Proc Natl Acad Sci U S A,
103,
1221-1226.
|
|
|
|
|
|
|
A.L.Forget,
M.M.Kudron,
D.A.McGrew,
M.A.Calmann,
C.A.Schiffer,
and
K.L.Knight
(2006).
RecA dimers serve as a functional unit for assembly of active nucleoprotein filaments.
|
| |
Biochemistry,
45,
13537-13542.
|
|
|
|
|
|
|
C.Joo,
S.A.McKinney,
M.Nakamura,
I.Rasnik,
S.Myong,
and
T.Ha
(2006).
Real-time observation of RecA filament dynamics with single monomer resolution.
|
| |
Cell,
126,
515-527.
|
|
|
|
|
|
|
C.Wiese,
J.M.Hinz,
R.S.Tebbs,
P.B.Nham,
S.S.Urbin,
D.W.Collins,
L.H.Thompson,
and
D.Schild
(2006).
Disparate requirements for the Walker A and B ATPase motifs of human RAD51D in homologous recombination.
|
| |
Nucleic Acids Res,
34,
2833-2843.
|
|
|
|
|
|
|
C.Wyman,
and
R.Kanaar
(2006).
DNA double-strand break repair: all's well that ends well.
|
| |
Annu Rev Genet,
40,
363-383.
|
|
|
|
|
|
|
C.Wyman
(2006).
Monomer networking activates recombinases.
|
| |
Structure,
14,
949-950.
|
|
|
|
|
|
|
E.H.Egelman
(2006).
RecA assembly, one molecule at a time.
|
| |
Structure,
14,
1600-1602.
|
|
|
|
|
|
|
J.M.Cox,
S.N.Abbott,
S.Chitteni-Pattu,
R.B.Inman,
and
M.M.Cox
(2006).
Complementation of one RecA protein point mutation by another. Evidence for trans catalysis of ATP hydrolysis.
|
| |
J Biol Chem,
281,
12968-12975.
|
|
|
|
|
|
|
M.J.Bennett,
M.R.Sawaya,
and
D.Eisenberg
(2006).
Deposition diseases and 3D domain swapping.
|
| |
Structure,
14,
811-824.
|
|
|
|
|
|
|
M.Kojic,
Q.Zhou,
M.Lisby,
and
W.K.Holloman
(2006).
Rec2 interplay with both Brh2 and Rad51 balances recombinational repair in Ustilago maydis.
|
| |
Mol Cell Biol,
26,
678-688.
|
|
|
|
|
|
|
M.Spies,
and
S.C.Kowalczykowski
(2006).
The RecA binding locus of RecBCD is a general domain for recruitment of DNA strand exchange proteins.
|
| |
Mol Cell,
21,
573-580.
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|
|
|
|
|
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N.Sarai,
W.Kagawa,
T.Kinebuchi,
A.Kagawa,
K.Tanaka,
K.Miyagawa,
S.Ikawa,
T.Shibata,
H.Kurumizaka,
and
S.Yokoyama
(2006).
Stimulation of Dmc1-mediated DNA strand exchange by the human Rad54B protein.
|
| |
Nucleic Acids Res,
34,
4429-4437.
|
|
|
|
|
|
|
R.Krishna,
G.P.Manjunath,
P.Kumar,
A.Surolia,
N.R.Chandra,
K.Muniyappa,
and
M.Vijayan
(2006).
Crystallographic identification of an ordered C-terminal domain and a second nucleotide-binding site in RecA: new insights into allostery.
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| |
Nucleic Acids Res,
34,
2186-2195.
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|
PDB code:
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R.Rajan,
J.W.Wisler,
and
C.E.Bell
(2006).
Probing the DNA sequence specificity of Escherichia coli RECA protein.
|
| |
Nucleic Acids Res,
34,
2463-2471.
|
|
|
|
|
|
|
V.E.Galkin,
Y.Wu,
X.P.Zhang,
X.Qian,
Y.He,
X.Yu,
W.D.Heyer,
Y.Luo,
and
E.H.Egelman
(2006).
The Rad51/RadA N-terminal domain activates nucleoprotein filament ATPase activity.
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| |
Structure,
14,
983-992.
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PDB code:
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X.Qian,
Y.He,
X.Ma,
M.N.Fodje,
P.Grochulski,
and
Y.Luo
(2006).
Calcium stiffens archaeal Rad51 recombinase from Methanococcus voltae for homologous recombination.
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| |
J Biol Chem,
281,
39380-39387.
|
|
|
PDB code:
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Y.Matsuo,
I.Sakane,
Y.Takizawa,
M.Takahashi,
and
H.Kurumizaka
(2006).
Roles of the human Rad51 L1 and L2 loops in DNA binding.
|
| |
FEBS J,
273,
3148-3159.
|
|
|
|
|
|
|
A.Ariza,
D.J.Richard,
M.F.White,
and
C.S.Bond
(2005).
Conformational flexibility revealed by the crystal structure of a crenarchaeal RadA.
|
| |
Nucleic Acids Res,
33,
1465-1473.
|
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|
PDB code:
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C.E.Bell
(2005).
Structure and mechanism of Escherichia coli RecA ATPase.
|
| |
Mol Microbiol,
58,
358-366.
|
|
|
|
|
|
|
C.Proudfoot,
and
R.McCulloch
(2005).
Distinct roles for two RAD51-related genes in Trypanosoma brucei antigenic variation.
|
| |
Nucleic Acids Res,
33,
6906-6919.
|
|
|
|
|
|
|
D.Ristic,
M.Modesti,
T.van der Heijden,
J.van Noort,
C.Dekker,
R.Kanaar,
and
C.Wyman
(2005).
Human Rad51 filaments on double- and single-stranded DNA: correlating regular and irregular forms with recombination function.
|
| |
Nucleic Acids Res,
33,
3292-3302.
|
|
|
|
|
|
|
D.V.Bugreev,
E.I.Golub,
A.Z.Stasiak,
A.Stasiak,
and
A.V.Mazin
(2005).
Activation of human meiosis-specific recombinase Dmc1 by Ca2+.
|
| |
J Biol Chem,
280,
26886-26895.
|
|
|
|
|
|
|
E.Skordalakes,
A.P.Brogan,
B.S.Park,
H.Kohn,
and
J.M.Berger
(2005).
Structural mechanism of inhibition of the Rho transcription termination factor by the antibiotic bicyclomycin.
|
| |
Structure,
13,
99.
|
|
|
PDB codes:
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G.V.Petukhova,
R.J.Pezza,
F.Vanevski,
M.Ploquin,
J.Y.Masson,
and
R.D.Camerini-Otero
(2005).
The Hop2 and Mnd1 proteins act in concert with Rad51 and Dmc1 in meiotic recombination.
|
| |
Nat Struct Mol Biol,
12,
449-453.
|
|
|
|
|
|
|
T.Akiba,
N.Ishii,
N.Rashid,
M.Morikawa,
T.Imanaka,
and
K.Harata
(2005).
Structure of RadB recombinase from a hyperthermophilic archaeon, Thermococcus kodakaraensis KOD1: an implication for the formation of a near-7-fold helical assembly.
|
| |
Nucleic Acids Res,
33,
3412-3423.
|
|
|
PDB codes:
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T.Kinebuchi,
W.Kagawa,
H.Kurumizaka,
and
S.Yokoyama
(2005).
Role of the N-terminal domain of the human DMC1 protein in octamer formation and DNA binding.
|
| |
J Biol Chem,
280,
28382-28387.
|
|
|
|
|
|
|
V.E.Galkin,
F.Esashi,
X.Yu,
S.Yang,
S.C.West,
and
E.H.Egelman
(2005).
BRCA2 BRC motifs bind RAD51-DNA filaments.
|
| |
Proc Natl Acad Sci U S A,
102,
8537-8542.
|
|
|
|
|
|
|
X.P.Zhang,
K.I.Lee,
J.A.Solinger,
K.Kiianitsa,
and
W.D.Heyer
(2005).
Gly-103 in the N-terminal domain of Saccharomyces cerevisiae Rad51 protein is critical for DNA binding.
|
| |
J Biol Chem,
280,
26303-26311.
|
|
|
|
|
|
|
Y.Wu,
X.Qian,
Y.He,
I.A.Moya,
and
Y.Luo
(2005).
Crystal structure of an ATPase-active form of Rad51 homolog from Methanococcus voltae. Insights into potassium dependence.
|
| |
J Biol Chem,
280,
722-728.
|
|
|
PDB code:
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|
S.Sauvageau,
M.Ploquin,
and
J.Y.Masson
(2004).
Exploring the multiple facets of the meiotic recombinase Dmc1.
|
| |
Bioessays,
26,
1151-1155.
|
|
|
|
|
|
|
W.D.Heyer,
and
R.Kanaar
(2004).
Recombination mechanisms; fortieth anniversary meeting of the Holliday model.
|
| |
Mol Cell,
16,
1-9.
|
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|
|
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
code is
shown on the right.
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