2l0i
From Proteopedia
Solution structure of Rtt103 CTD-interacting domain bound to a Ser2 phosphorylated CTD peptide
Structural highlights
Function[RT103_YEAST] Involved in transcription termination by RNA polymerase II and in regulation of Ty1 transposition.[1] [2] Evolutionary ConservationCheck, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedPhosphorylation of the C-terminal domain (CTD) of RNA polymerase II controls the co-transcriptional assembly of RNA processing and transcription factors. Recruitment relies on conserved CTD-interacting domains (CIDs) that recognize different CTD phosphoisoforms during the transcription cycle, but the molecular basis for their specificity remains unclear. We show that the CIDs of two transcription termination factors, Rtt103 and Pcf11, achieve high affinity and specificity both by specifically recognizing the phosphorylated CTD and by cooperatively binding to neighboring CTD repeats. Single-residue mutations at the protein-protein interface abolish cooperativity and affect recruitment at the 3' end processing site in vivo. We suggest that this cooperativity provides a signal-response mechanism to ensure that its action is confined only to proper polyadenylation sites where Ser2 phosphorylation density is highest. Cooperative interaction of transcription termination factors with the RNA polymerase II C-terminal domain.,Lunde BM, Reichow SL, Kim M, Suh H, Leeper TC, Yang F, Mutschler H, Buratowski S, Meinhart A, Varani G Nat Struct Mol Biol. 2010 Oct;17(10):1195-201. Epub 2010 Sep 5. PMID:20818393[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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Categories: Atcc 18824 | Large Structures | Buratowski, S | Kim, M | Leeper, T C | Lunde, B M | Meinhart, A | Mutschler, H | Reichow, S L | Suh, H | Varani, G | Yang, F | 3' end processing | Transcription