Cooperation between intrinsically disordered and ordered
regions of Spt6 regulates nucleosome and Pol II CTD binding,
and nucleosome assembly

J 2022

Cooperation between intrinsically disordered and ordered regions of Spt6 regulates nucleosome and Pol II CTD binding, and nucleosome assembly

KASILIAUSKAITE, Aiste, Karel KUBÍČEK, Tomáš KLUMPLER, Martina ZÁNOVÁ, David ZAPLETAL et. al.

Základní údaje

Originální název

Cooperation between intrinsically disordered and ordered regions of Spt6 regulates nucleosome and Pol II CTD binding, and nucleosome assembly

Autoři

KASILIAUSKAITE, Aiste (440 Litva, domácí), Karel KUBÍČEK (203 Česká republika, domácí), Tomáš KLUMPLER (203 Česká republika, domácí), Martina ZÁNOVÁ (703 Slovensko, domácí), David ZAPLETAL (203 Česká republika, domácí), Eliska KOUTNA, Jiří NOVÁČEK (203 Česká republika, domácí) a Richard ŠTEFL (203 Česká republika, garant, domácí)

Vydání

Nucleic acids research, Oxford, Oxford University Press, 2022, 0305-1048

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10608 Biochemistry and molecular biology

Stát vydavatele

Velká Británie a Severní Irsko

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 14.900

Kód RIV

RIV/00216224:14740/22:00127507

Organizační jednotka

Středoevropský technologický institut

DOI

http://dx.doi.org/10.1093/nar/gkac451

UT WoS

000805243900001

Klíčová slova anglicky

RNA polymerase II; transcription elongation factor; transcription elongation factor Spt6; unclassified drug

Štítky

CF CRYO, CF PROT, CF SAXS, rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 27. 10. 2024 14:23, Ing. Martina Blahová

Anotace

V originále

Transcription elongation factor Spt6 associates with RNA polymerase II (Pol II) and acts as a histone chaperone, which promotes the reassembly of nucleosomes following the passage of Pol II. The precise mechanism of nucleosome reassembly mediated by Spt6 remains unclear. In this study, we used a hybrid approach combining cryo-electron microscopy and small-angle X-ray scattering to visualize the architecture of Spt6 from Saccharomyces cerevisiae. The reconstructed overall architecture of Spt6 reveals not only the core of Spt6, but also its flexible N- and C-termini, which are critical for Spt6’s function. We found that the acidic N-terminal region of Spt6 prevents the binding of Spt6 not only to the Pol II CTD and Pol II CTD-linker, but also to pre-formed intact nucleosomes and nucleosomal DNA. The N-terminal region of Spt6 self-associates with the tSH2 domain and the core of Spt6 and thus controls binding to Pol II and nucleosomes. Furthermore, we found that Spt6 promotes the assembly of nucleosomes in vitro. These data indicate that the cooperation between the intrinsically disordered and structured regions of Spt6 regulates nucleosome and Pol II CTD binding, and also nucleosome assembly.

Návaznosti

GA22-19896S, projekt VaV

Název: Strukturní podstata pro opětovné sestavení nukleosomu při přepisu genu zprostředkovaná proteinem Spt6

Investor: Grantová agentura ČR, Strukturní podstata pro opětovné sestavení nukleosomu při přepisu genu zrostředkovaná proteinem Spt6

LQ1601, projekt VaV

Název: CEITEC 2020 (Akronym: CEITEC2020)

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

649030, interní kód MU

Název: DECOR - Dynamic assembly and exchange of RNA polymerase II CTD factors (Akronym: DECOR)

Investor: Evropská unie, DECOR - Dynamic assembly and exchange of RNA polymerase II CTD factors, ERC (Excellent Science)

90127, velká výzkumná infrastruktura

Název: CIISB II

Citovat

KASILIAUSKAITE, Aiste, Karel KUBÍČEK, Tomáš KLUMPLER, Martina ZÁNOVÁ, David ZAPLETAL, Eliska KOUTNA, Jiří NOVÁČEK a Richard ŠTEFL. Cooperation between intrinsically disordered and ordered regions of Spt6 regulates nucleosome and Pol II CTD binding, and nucleosome assembly. Nucleic acids research. Oxford: Oxford University Press, 2022, roč. 50, č. 10, s. 5961-5973. ISSN 0305-1048. Dostupné z: https://dx.doi.org/10.1093/nar/gkac451.

@article{2240862,
   author = {Kasiliauskaite, Aiste and Kubíček, Karel and Klumpler, Tomáš and Zánová, Martina and Zapletal, David and Koutna, Eliska and Nováček, Jiří and Štefl, Richard},
   article_location = {Oxford},
   article_number = {10},
   doi = {http://dx.doi.org/10.1093/nar/gkac451},
   keywords = {RNA polymerase II; transcription elongation factor; transcription elongation factor Spt6; unclassified drug},
   language = {eng},
   issn = {0305-1048},
   journal = {Nucleic acids research},
   title = {Cooperation between intrinsically disordered and ordered regions of Spt6 regulates nucleosome and Pol II CTD binding, and nucleosome assembly},
   url = {https://academic.oup.com/nar/article/50/10/5961/6595227?login=true},
   volume = {50},
   year = {2022}
}

TY  - JOUR
ID  - 2240862
AU  - Kasiliauskaite, Aiste - Kubíček, Karel - Klumpler, Tomáš - Zánová, Martina - Zapletal, David - Koutna, Eliska - Nováček, Jiří - Štefl, Richard
PY  - 2022
TI  - Cooperation between intrinsically disordered and ordered regions of Spt6 regulates nucleosome and Pol II CTD binding, and nucleosome assembly
JF  - Nucleic acids research
VL  - 50
IS  - 10
SP  - 5961-5973
EP  - 5961-5973
PB  - Oxford University Press
SN  - 03051048
KW  - RNA polymerase II
KW  - transcription elongation factor
KW  - transcription elongation factor Spt6
KW  - unclassified drug
UR  - https://academic.oup.com/nar/article/50/10/5961/6595227?login=true
N2  - Transcription elongation factor Spt6 associates with RNA polymerase II (Pol II) and acts as a histone chaperone, which promotes the reassembly of nucleosomes following the passage of Pol II. The precise mechanism of nucleosome reassembly mediated by Spt6 remains unclear. In this study, we used a hybrid approach combining cryo-electron microscopy and small-angle X-ray scattering to visualize the architecture of Spt6 from Saccharomyces cerevisiae. The reconstructed overall architecture of Spt6 reveals not only the core of Spt6, but also its flexible N- and C-termini, which are critical for Spt6’s function. We found that the acidic N-terminal region of Spt6 prevents the binding of Spt6 not only to the Pol II CTD and Pol II CTD-linker, but also to pre-formed intact nucleosomes and nucleosomal DNA. The N-terminal region of Spt6 self-associates with the tSH2 domain and the core of Spt6 and thus controls binding to Pol II and nucleosomes. Furthermore, we found that Spt6 promotes the assembly of nucleosomes in vitro. These data indicate that the cooperation between the intrinsically disordered and structured regions of Spt6 regulates nucleosome and Pol II CTD binding, and also nucleosome assembly.
ER  -

KASILIAUSKAITE, Aiste, Karel KUBÍČEK, Tomáš KLUMPLER, Martina ZÁNOVÁ, David ZAPLETAL, Eliska KOUTNA, Jiří NOVÁČEK a Richard ŠTEFL. Cooperation between intrinsically disordered and ordered regions of Spt6 regulates nucleosome and Pol II CTD binding, and nucleosome assembly. \textit{Nucleic acids research}. Oxford: Oxford University Press, 2022, roč.~50, č.~10, s.~5961-5973. ISSN~0305-1048. Dostupné z: https://dx.doi.org/10.1093/nar/gkac451.

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