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@proceedings{1376987,
author = {Jasnovidova, Olga and Krejčíková, Magdaléna and Kubíček, Karel and Štefl, Richard},
booktitle = {41st FEBS Congress on Molecular and Systems Biology for a Better Life},
keywords = {NMR ; RNA processing; RNAPII; CTD code; structural biology; phosphorylation; Rtt103p},
language = {eng},
title = {Recognition of phosphorylated threonine-4 of RNA polymerase II C-terminal domain by 3 '-end processing apparatus},
year = {2016}
}
TY - CONF
ID - 1376987
AU - Jasnovidova, Olga - Krejčíková, Magdaléna - Kubíček, Karel - Štefl, Richard
PY - 2016
TI - Recognition of phosphorylated threonine-4 of RNA polymerase II C-terminal domain by 3 '-end processing apparatus
KW - NMR
KW - RNA processing
KW - RNAPII
KW - CTD code
KW - structural biology
KW - phosphorylation
KW - Rtt103p
N2 - Phosphorylation patterns of the C-terminal domain (CTD) of largest subunit of RNA polymerase II (called the CTD code) orchestrate the recruitment of RNA processing and transcription factors. Recent studies showed that not only serines and tyrosines but also threonines of the CTD can be phosphorylated with a number of functional consequences, including the interaction with yeast transcription termination factor, Rtt103p. Here, we report the solution structure of the Rtt103p CTD-interacting domain (CID) bound to Thr4 phosphorylated CTD, a poorly understood letter of the CTD code. The structure reveals a direct recognition of the phospho-Thr4 mark by Rtt103p CID and extensive interactions involving residues from three repeats of the CTD heptad. Intriguingly, Rtt103p's CID binds equally well Thr4 and Ser2 phosphorylated CTD A doubly phosphorylated CTD at Ser2 and Thr4 diminishes its binding affinity due to electrostatic repulsion. Our structural data suggest that the recruitment of a CID-containing CTD-binding factor may be coded by more than one letter of the CTD code.
ER -
JASNOVIDOVA, Olga, Magdaléna KREJČÍKOVÁ, Karel KUBÍČEK a Richard ŠTEFL. Recognition of phosphorylated threonine-4 of RNA polymerase II C-terminal domain by 3 '-end processing apparatus. Online. In \textit{41st FEBS Congress on Molecular and Systems Biology for a Better Life}. 2016. ISSN~1742-464X. [citováno 2024-04-23]
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