Architecture of TAF11/TAF13/TBP complex suggests novel regulation properties of general transcription factor TFIID

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F17%3A00482733" target="_blank" >RIV/61388971:_____/17:00482733 - isvavai.cz</a>

Alternative codes found

RIV/00216208:11310/17:10366587

Result on the web

<a href="http://dx.doi.org/10.7554/eLife.30395" target="_blank" >http://dx.doi.org/10.7554/eLife.30395</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.7554/eLife.30395" target="_blank" >10.7554/eLife.30395</a>

Result language

angličtina

Original language name

Architecture of TAF11/TAF13/TBP complex suggests novel regulation properties of general transcription factor TFIID

Original language description

General transcription factor TFIID is a key component of RNA polymerase II transcription initiation. Human TFIID is a megadalton-sized complex comprising TATA-binding protein (TBP) and 13 TBP-associated factors (TAFs). TBP binds to core promoter DNA, recognizing the TATA-box. We identified a ternary complex formed by TBP and the histone fold (HF) domain containing TFIID subunits TAF11 and TAF13. We demonstrate that TAF11/TAF13 competes for TBP binding with TATA-box DNA, and also with the N-terminal domain of TAF1 previously implicated in TATA-box mimicry. In an integrative approach combining crystal coordinates, biochemical analyses and data from cross-linking mass-spectrometry (CLMS), we determine the architecture of the TAF11/TAF13/TBP complex, revealing TAF11/TAF13 interaction with the DNA binding surface of TBP. We identify a highly conserved C-terminal TBP-interaction domain (CTID) in TAF13, which is essential for supporting cell growth. Our results thus have implications for cellular TFIID assembly and suggest a novel regulatory state for TFIID function.

Czech name

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Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

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OECD FORD branch

10608 - Biochemistry and molecular biology

Project

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Continuities

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2017

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

eLife

ISSN

2050-084X

e-ISSN

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Volume of the periodical

6

Issue of the periodical within the volume

e30395

Country of publishing house

GB - UNITED KINGDOM

Number of pages

31

Pages from-to

1-31

UT code for WoS article

000415304700001

EID of the result in the Scopus database

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