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@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 and 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, vol.~50, No~10, p.~5961-5973. ISSN~0305-1048. Available from: https://dx.doi.org/10.1093/nar/gkac451.
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