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6DRD

RNA Pol II(G)

Summary for 6DRD
Entry DOI10.2210/pdb6drd/pdb
EMDB information7997 7998
DescriptorDNA-directed RNA polymerase II subunit RPB1, DNA-directed RNA polymerases I, II, and III subunit RPABC5, DNA-directed RNA polymerase II subunit RPB11-a, ... (14 entities in total)
Functional Keywordsrna pol ii(g), gdown1, transcription repression, molecular mechanism, transferase
Biological sourceHomo sapiens (Human)
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Total number of polymer chains13
Total formula weight523566.62
Authors
Yu, X.,Jishage, M.,Shi, Y.,Ganesan, S.,Sali, A.,Chait, B.T.,Asturias, F.,Roeder, R.G. (deposition date: 2018-06-11, release date: 2019-06-12, Last modification date: 2019-12-04)
Primary citationJishage, M.,Yu, X.,Shi, Y.,Ganesan, S.J.,Chen, W.Y.,Sali, A.,Chait, B.T.,Asturias, F.J.,Roeder, R.G.
Architecture of Pol II(G) and molecular mechanism of transcription regulation by Gdown1.
Nat. Struct. Mol. Biol., 25:859-867, 2018
Cited by
PubMed Abstract: Tight binding of Gdown1 represses RNA polymerase II (Pol II) function in a manner that is reversed by Mediator, but the structural basis of these processes is unclear. Although Gdown1 is intrinsically disordered, its Pol II interacting domains were localized and shown to occlude transcription factor IIF (TFIIF) and transcription factor IIB (TFIIB) binding by perfect positioning on their Pol II interaction sites. Robust binding of Gdown1 to Pol II is established by cooperative interactions of a strong Pol II binding region and two weaker binding modulatory regions, thus providing a mechanism both for tight Pol II binding and transcription inhibition and for its reversal. In support of a physiological function for Gdown1 in transcription repression, Gdown1 co-localizes with Pol II in transcriptionally silent nuclei of early Drosophila embryos but re-localizes to the cytoplasm during zygotic genome activation. Our study reveals a self-inactivation through Gdown1 binding as a unique mode of repression in Pol II function.
PubMed: 30190596
DOI: 10.1038/s41594-018-0118-5
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.9 Å)
Structure validation

226707

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