What are the key aspects of interaction between RNA polymerase
II C-terminal domain phosphorylated on tyrosine-1 and the
elongation factors

a 2016

What are the key aspects of interaction between RNA polymerase II C-terminal domain phosphorylated on tyrosine-1 and the elongation factors

KUBÍČEK, Karel; Magdaléna KREJČÍKOVÁ; Pavel BRÁZDA; Eliška ŠMIŘÁKOVÁ; Jiří NOVÁČEK et. al.

Základní údaje

Originální název

What are the key aspects of interaction between RNA polymerase II C-terminal domain phosphorylated on tyrosine-1 and the elongation factors

Autoři

KUBÍČEK, Karel (203 Česká republika, domácí); Magdaléna KREJČÍKOVÁ (203 Česká republika, domácí); Pavel BRÁZDA (203 Česká republika, domácí); Eliška ŠMIŘÁKOVÁ (203 Česká republika, domácí); Jiří NOVÁČEK (203 Česká republika, domácí); Patrick CRAMER (276 Německo) a Richard ŠTEFL (203 Česká republika, garant, domácí)

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

Kód RIV

RIV/00216224:14740/16:00096391

Organizační jednotka

Středoevropský technologický institut

ISSN

UT WoS

000383616900059

Klíčová slova anglicky

RNA polymerase II; CTD; tSH2 Spt6; elongation factor; structural biology; NMR; transcription

Štítky

rivok

Změněno: 9. 11. 2017 09:03, Mgr. Eva Špillingová

Anotace

V originále

Post-translational modifications of the consensus motif Y1-S2-P3-T4-S5-P6-S7 of the C-terminal domain (CTD) of RNA polymerase II are since last decade known as the “CTD code”. These modifications are dynamic and specific for each phase of the transcriptional cycle. Increased phosphorylation levels of Y1 during the productive elongation prevents binding of termination factors, and stimulates recruitment of elongation factors. However, there is no structural information on how the phosphotyrosine modified CTD is recognized by these elongation factors. To investigate phosphotyrosine recognition, we employed integrative approach to structural biology–namely combination of solution nuclear magnetic resonance, small angle X-ray scattering, mass spectrometry and X-ray crystallography, supported by functional studies with point/multiple mutations. We will present the structural data for phosphotyrosine recognition within the CTD by the elongation factor, which help to decipher how this important CTD modification mark is read out by transcription factors.

Návaznosti

LQ1601, projekt VaV

Název: CEITEC 2020 (Akronym: CEITEC2020)

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

Citovat

KUBÍČEK, Karel; Magdaléna KREJČÍKOVÁ; Pavel BRÁZDA; Eliška ŠMIŘÁKOVÁ; Jiří NOVÁČEK; Patrick CRAMER a Richard ŠTEFL. What are the key aspects of interaction between RNA polymerase II C-terminal domain phosphorylated on tyrosine-1 and the elongation factors. In 41st FEBS Congress on Molecular and Systems Biology for a Better Life. 2016. ISSN 1742-464X.

@proceedings{1376986,
   author = {Kubíček, Karel and Krejčíková, Magdaléna and Brázda, Pavel and Šmiřáková, Eliška and Nováček, Jiří and Cramer, Patrick and Štefl, Richard},
   booktitle = {41st FEBS Congress on Molecular and Systems Biology for a Better Life},
   keywords = {RNA polymerase II; CTD; tSH2 Spt6; elongation factor; structural biology; NMR; transcription},
   language = {eng},
   title = {What are the key aspects of interaction between RNA polymerase II C-terminal domain phosphorylated on tyrosine-1 and the elongation factors},
   year = {2016}
}

TY  - CONF
ID  - 1376986
AU  - Kubíček, Karel - Krejčíková, Magdaléna - Brázda, Pavel - Šmiřáková, Eliška - Nováček, Jiří - Cramer, Patrick - Štefl, Richard
PY  - 2016
TI  - What are the key aspects of interaction between RNA polymerase II C-terminal domain phosphorylated on tyrosine-1 and the elongation factors
KW  - RNA polymerase II
KW  - CTD
KW  - tSH2 Spt6
KW  - elongation factor
KW  - structural biology
KW  - NMR
KW  - transcription
N2  - Post-translational modifications of the consensus motif Y1-S2-P3-T4-S5-P6-S7 of the C-terminal domain (CTD) of RNA polymerase II are since last decade known as the “CTD code”. These modifications are dynamic and specific for each phase of the transcriptional cycle. Increased phosphorylation levels of Y1 during the productive elongation prevents binding of termination factors, and stimulates recruitment of elongation factors. However, there is no structural information on how the phosphotyrosine modified CTD is recognized by these elongation factors. To investigate phosphotyrosine recognition, we employed integrative approach to structural biology–namely combination of solution nuclear magnetic resonance, small angle X-ray scattering, mass spectrometry and X-ray crystallography, supported by functional studies with point/multiple mutations. We will present the structural data for phosphotyrosine recognition within the CTD by the elongation factor, which help to decipher how this important CTD modification mark is read out by transcription factors.
ER  -

KUBÍČEK, Karel; Magdaléna KREJČÍKOVÁ; Pavel BRÁZDA; Eliška ŠMIŘÁKOVÁ; Jiří NOVÁČEK; Patrick CRAMER a Richard ŠTEFL. What are the key aspects of interaction between RNA polymerase II C-terminal domain phosphorylated on tyrosine-1 and the elongation factors. In \textit{41st FEBS Congress on Molecular and Systems Biology for a Better Life}. 2016. ISSN~1742-464X.

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