Recognition of phosphorylated threonine-4 of RNA polymerase II
C-terminal domain by 3 '-end processing apparatus

a 2016

Recognition of phosphorylated threonine-4 of RNA polymerase II C-terminal domain by 3 '-end processing apparatus

JASNOVIDOVA, Olga; Magdaléna KREJČÍKOVÁ; Karel KUBÍČEK a Richard ŠTEFL

Základní údaje

Originální název

Recognition of phosphorylated threonine-4 of RNA polymerase II C-terminal domain by 3 '-end processing apparatus

Autoři

JASNOVIDOVA, Olga; Magdaléna KREJČÍKOVÁ; Karel KUBÍČEK a Richard ŠTEFL

Vydání

41st FEBS Congress on Molecular and Systems Biology for a Better Life, 2016

Další údaje

Jazyk

angličtina

Typ výsledku

Konferenční abstrakt

Obor

10600 1.6 Biological sciences

Stát vydavatele

Spojené státy

Utajení

není předmětem státního či obchodního tajemství

Impakt faktor

Impact factor: 3.902

Označené pro přenos do RIV

Ano

Kód RIV

RIV/00216224:14740/16:00096392

Organizační jednotka

Středoevropský technologický institut

ISSN

UT WoS

000383616901250

Klíčová slova anglicky

NMR ; RNA processing; RNAPII; CTD code; structural biology; phosphorylation; Rtt103p

Štítky

rivok

Změněno: 8. 11. 2017 16:29, Mgr. Eva Špillingová

Anotace

V originále

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.

Návaznosti

LQ1601, projekt VaV

Název: CEITEC 2020 (Akronym: CEITEC2020)

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, CEITEC 2020

Citovat

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. In 41st FEBS Congress on Molecular and Systems Biology for a Better Life. 2016. ISSN 1742-464X.

@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. In \textit{41st FEBS Congress on Molecular and Systems Biology for a Better Life}. 2016. ISSN~1742-464X.

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