2KM4

Solution structure of Rtt103 CTD interacting domain

2KM4 の概要

• エントリーDOI: 10.2210/pdb2km4/pdb
• NMR情報: BMRB: 16411
• 分子名称: Regulator of Ty1 transposition protein 103 (1 entity in total)
• 機能のキーワード: ctd-interacting domain, rna polymerase ii binding protein, phosphoprotein, transcription termination, dna-binding, nucleus, transcription, transcription regulation, transcription regulator
• 由来する生物種: Saccharomyces cerevisiae (yeast)
• 細胞内の位置: Nucleus: Q05543
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 16569.10

構造登録者

Lunde, B.M.,Reichow, S.,Kim, M.,Leeper, T.C.,Becker, R.,Buratowski, S.,Meinhart, A.,Varani, G. (登録日: 2009-07-20, 公開日: 2010-09-08, 最終更新日: 2024-05-01)

主引用文献

Lunde, B.M.,Reichow, S.L.,Kim, M.,Suh, H.,Leeper, T.C.,Yang, F.,Mutschler, H.,Buratowski, S.,Meinhart, A.,Varani, G.
Cooperative interaction of transcription termination factors with the RNA polymerase II C-terminal domain.
Nat.Struct.Mol.Biol., 17:1195-1201, 2010

PubMed Abstract: Phosphorylation 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.

PubMed: 20818393
DOI: 10.1038/nsmb.1893

実験手法

SOLUTION NMR