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* Residue conservation analysis
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PDB id:
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Transcription
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Title:
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Structure of the schizosaccharomyces pombe mediator subcomplex med8c/18
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Structure:
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Mediator of RNA polymerase ii transcription subunit 18. Chain: a. Synonym: mediator complex subunit 18, cell separation protein sep11, RNA polymerase ii mediator complex protein pmc6. Engineered: yes. Mediator of RNA polymerase ii transcription subunit 8. Chain: b. Fragment: c-terminal domain, unp residues 180-200. Synonym: mediator complex subunit 8, cell separation protein sep15.
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Source:
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Schizosaccharomyces pombe. Fission yeast. Organism_taxid: 4896. Gene: med18. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: med8.
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Resolution:
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2.40Å
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R-factor:
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0.211
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R-free:
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0.231
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Authors:
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L.Lariviere,M.Seizl,S.Van Wageningen,S.Roether,L.Van De Pasch, H.Feldmann,K.Straesser,S.Hahn,C.P.Holstege,P.Cramer
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Key ref:
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L.Larivière
et al.
(2008).
Structure-system correlation identifies a gene regulatory Mediator submodule.
Genes Dev,
22,
872-877.
PubMed id:
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Date:
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21-Jan-08
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Release date:
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22-Apr-08
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PROCHECK
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Headers
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References
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Enzyme class:
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Chains A, B:
E.C.?
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Genes Dev
22:872-877
(2008)
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PubMed id:
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Structure-system correlation identifies a gene regulatory Mediator submodule.
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L.Larivière,
M.Seizl,
S.van Wageningen,
S.Röther,
L.van de Pasch,
H.Feldmann,
K.Strässer,
S.Hahn,
F.C.Holstege,
P.Cramer.
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ABSTRACT
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A combination of crystallography, biochemistry, and gene expression analysis
identifies the coactivator subcomplex Med8C/18/20 as a functionally distinct
submodule of the Mediator head module. Med8C forms a conserved alpha-helix that
tethers Med18/20 to the Mediator. Deletion of Med8C in vivo results in
dissociation of Med18/20 from Mediator and in loss of transcription activity of
extracts. Deletion of med8C, med18, or med20 causes similar changes in the yeast
transcriptome, establishing Med8C/18/20 as a predominantly positive,
gene-specific submodule required for low transcription levels of nonactivated
genes, including conjugation genes. The presented structure-based system
perturbation is superior to gene deletion analysis of gene regulation.
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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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L.Larivière,
C.Plaschka,
M.Seizl,
L.Wenzeck,
F.Kurth,
and
P.Cramer
(2012).
Structure of the Mediator head module.
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Nature,
492,
448-451.
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PDB codes:
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E.Czeko,
M.Seizl,
C.Augsberger,
T.Mielke,
and
P.Cramer
(2011).
Iwr1 directs RNA polymerase II nuclear import.
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Mol Cell,
42,
261-266.
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E.Vojnic,
A.Mourão,
M.Seizl,
B.Simon,
L.Wenzeck,
L.Larivière,
S.Baumli,
K.Baumgart,
M.Meisterernst,
M.Sattler,
and
P.Cramer
(2011).
Structure and VP16 binding of the Mediator Med25 activator interaction domain.
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Nat Struct Mol Biol,
18,
404-409.
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PDB code:
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P.Cramer
(2010).
Towards molecular systems biology of gene transcription and regulation.
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Biol Chem,
391,
731-735.
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T.Koschubs,
K.Lorenzen,
S.Baumli,
S.Sandström,
A.J.Heck,
and
P.Cramer
(2010).
Preparation and topology of the Mediator middle module.
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Nucleic Acids Res,
38,
3186-3195.
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E.T.Young,
K.Yen,
K.M.Dombek,
G.L.Law,
E.Chang,
and
E.Arms
(2009).
Snf1-independent, glucose-resistant transcription of Adr1-dependent genes in a mediator mutant of Saccharomyces cerevisiae.
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Mol Microbiol,
74,
364-383.
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H.Takahashi,
K.Kasahara,
and
T.Kokubo
(2009).
Saccharomyces cerevisiae Med9 comprises two functionally distinct domains that play different roles in transcriptional regulation.
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Genes Cells,
14,
53-67.
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T.Koschubs,
M.Seizl,
L.Larivière,
F.Kurth,
S.Baumli,
D.E.Martin,
and
P.Cramer
(2009).
Identification, structure, and functional requirement of the Mediator submodule Med7N/31.
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EMBO J,
28,
69-80.
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PDB codes:
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T.Margaritis,
P.Lijnzaad,
D.van Leenen,
D.Bouwmeester,
P.Kemmeren,
S.R.van Hooff,
and
F.C.Holstege
(2009).
Adaptable gene-specific dye bias correction for two-channel DNA microarrays.
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Mol Syst Biol,
5,
266.
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Z.Shaikhibrahim,
H.Rahaman,
P.Wittung-Stafshede,
and
S.Björklund
(2009).
Med8, Med18, and Med20 subunits of the Mediator head domain are interdependent upon each other for folding and complex formation.
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Proc Natl Acad Sci U S A,
106,
20728-20733.
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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
codes are
shown on the right.
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Links
