A Structural Basis for the Cross-Talk Between Histones and RNA Polymerase II

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F20%3A00118407" target="_blank" >RIV/00216224:14740/20:00118407 - isvavai.cz</a>

Výsledek na webu

<a href="https://www.ceitec.eu/abstract-book-final-docx-pdf/f36324" target="_blank" >https://www.ceitec.eu/abstract-book-final-docx-pdf/f36324</a>

DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

A Structural Basis for the Cross-Talk Between Histones and RNA Polymerase II

Popis výsledku v původním jazyce

Transcription of eukaryotic protein-coding genes requires transfer of RNA polymerase II (Pol II) through nucleosomes. Nucleosomes are inherent barriers of transcription, and Pol II stalls at multiple locations within a nucleosome. Nucleosome core particle (NCP) consists of 145–147 base pairs of DNA wrapped around a histone protein octamer. Transcription elongation factors accompany Pol II to facilitate efficient transcription. They enable polymerase progression through NCPs and ensure re-establishment of chromatin after polymerase passage. The mechanisms underlying these processes, however, remain puzzling and poorly understood. Our aim is to present molecular details underlying Spt6 (histone chaperone and transcription factor) binding events. In our study we are revealing this long-standing open question by identifying elements of Spt6 that mediates interactions between Pol II and nucleosome. Cryo-electron microscopy, X-ray and Small Angle X-ray Scattering (SAXS) are used to study the macromolecular complex. Our findings provide a fundamental mechanistic insight into the functional specialization of Spt6 and have implications for the understanding of crosstalk between RNAP II and chromosomes.

Název v anglickém jazyce

A Structural Basis for the Cross-Talk Between Histones and RNA Polymerase II

Popis výsledku anglicky

Transcription of eukaryotic protein-coding genes requires transfer of RNA polymerase II (Pol II) through nucleosomes. Nucleosomes are inherent barriers of transcription, and Pol II stalls at multiple locations within a nucleosome. Nucleosome core particle (NCP) consists of 145–147 base pairs of DNA wrapped around a histone protein octamer. Transcription elongation factors accompany Pol II to facilitate efficient transcription. They enable polymerase progression through NCPs and ensure re-establishment of chromatin after polymerase passage. The mechanisms underlying these processes, however, remain puzzling and poorly understood. Our aim is to present molecular details underlying Spt6 (histone chaperone and transcription factor) binding events. In our study we are revealing this long-standing open question by identifying elements of Spt6 that mediates interactions between Pol II and nucleosome. Cryo-electron microscopy, X-ray and Small Angle X-ray Scattering (SAXS) are used to study the macromolecular complex. Our findings provide a fundamental mechanistic insight into the functional specialization of Spt6 and have implications for the understanding of crosstalk between RNAP II and chromosomes.

Druh

O - Ostatní výsledky

CEP obor

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OECD FORD obor

10608 - Biochemistry and molecular biology

Projekt

<a href="/cs/project/LQ1601" target="_blank" >LQ1601: CEITEC 2020</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2020

Kód důvěrnosti údajů

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