Structural insight into recognition of phosphorylated
threonine-4 of RNA polymerase II C-terminal domain by Rtt103p

J 2017

Structural insight into recognition of phosphorylated threonine-4 of RNA polymerase II C-terminal domain by Rtt103p

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

Základní údaje

Originální název

Structural insight into recognition of phosphorylated threonine-4 of RNA polymerase II C-terminal domain by Rtt103p

Autoři

JASNOVIDOVA, Olga (233 Estonsko, domácí), Magdaléna KREJČÍKOVÁ (203 Česká republika, domácí), Karel KUBÍČEK (203 Česká republika, domácí) a Richard ŠTEFL (203 Česká republika, garant, domácí)

Vydání

EMBO reports, Hoboken, Wiley-Blackwell, 2017, 1469-221X

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10600 1.6 Biological sciences

Stát vydavatele

Spojené státy

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 8.749

Kód RIV

RIV/00216224:14740/17:00094697

Organizační jednotka

Středoevropský technologický institut

DOI

http://dx.doi.org/10.15252/embr.201643723

UT WoS

000402606700012

Klíčová slova anglicky

NMR; RNA processing; RNAPII CTD code; structural biology

Štítky

CF NMR, OA, rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 23. 2. 2018 13:48, Mgr. Pavla Foltynová, Ph.D.

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

GA13-18344S, projekt VaV

Název: Studium kódu CTD RNA polymerázy II

Investor: Grantová agentura ČR, Studium kódu CTD RNA polymerázy II

GA15-24117S, projekt VaV

Název: Zásadní význam fosforylace YS. Studium interakce mezi CTD a transkripčním elongačním faktorem Spt6

Investor: Grantová agentura ČR, Zásadní význam fosforylace YS. Studium interakce mezi CTD a transkripčním elongačním faktorem Spt6

LM2015043, projekt VaV

Název: Česká infrastruktura pro integrativní strukturní biologii (Akronym: CIISB)

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Czech Infrastructure for Integrative Structural Biology

LQ1601, projekt VaV

Název: CEITEC 2020 (Akronym: CEITEC2020)

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

Přiložené soubory

embr.201643723.pdf

Vyhledat podobné dokumenty

Citovat

JASNOVIDOVA, Olga, Magdaléna KREJČÍKOVÁ, Karel KUBÍČEK a Richard ŠTEFL. Structural insight into recognition of phosphorylated threonine-4 of RNA polymerase II C-terminal domain by Rtt103p. EMBO reports. Hoboken: Wiley-Blackwell, 2017, roč. 18, č. 6, s. 906-913. ISSN 1469-221X. Dostupné z: https://dx.doi.org/10.15252/embr.201643723.

@article{1376840,
   author = {Jasnovidova, Olga and Krejčíková, Magdaléna and Kubíček, Karel and Štefl, Richard},
   article_location = {Hoboken},
   article_number = {6},
   doi = {http://dx.doi.org/10.15252/embr.201643723},
   keywords = {NMR; RNA processing; RNAPII CTD code; structural biology},
   language = {eng},
   issn = {1469-221X},
   journal = {EMBO reports},
   title = {Structural insight into recognition of phosphorylated threonine-4 of RNA polymerase II C-terminal domain by Rtt103p},
   url = {http://embor.embopress.org/content/18/6/906},
   volume = {18},
   year = {2017}
}

TY  - JOUR
ID  - 1376840
AU  - Jasnovidova, Olga - Krejčíková, Magdaléna - Kubíček, Karel - Štefl, Richard
PY  - 2017
TI  - Structural insight into recognition of phosphorylated threonine-4 of RNA polymerase II C-terminal domain by Rtt103p
JF  - EMBO reports
VL  - 18
IS  - 6
SP  - 906-913
EP  - 906-913
PB  - Wiley-Blackwell
SN  - 1469221X
KW  - NMR
KW  - RNA processing
KW  - RNAPII CTD code
KW  - structural biology
UR  - http://embor.embopress.org/content/18/6/906
L2  - http://embor.embopress.org/content/18/6/906
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. Structural insight into recognition of phosphorylated threonine-4 of RNA polymerase II C-terminal domain by Rtt103p. \textit{EMBO reports}. Hoboken: Wiley-Blackwell, 2017, roč.~18, č.~6, s.~906-913. ISSN~1469-221X. Dostupné z: https://dx.doi.org/10.15252/embr.201643723.

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