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Chromatin remodeller Fun30Fft3 induces nucleosome disassembly to facilitate RNA polymerase II elongation.


ABSTRACT: Previous studies have revealed that nucleosomes impede elongation of RNA polymerase II (RNAPII). Recent observations suggest a role for ATP-dependent chromatin remodellers in modulating this process, but direct in vivo evidence for this is unknown. Here using fission yeast, we identify Fun30Fft3 as a chromatin remodeller, which localizes at transcribing regions to promote RNAPII transcription. Fun30Fft3 associates with RNAPII and collaborates with the histone chaperone, FACT, which facilitates RNAPII elongation through chromatin, to induce nucleosome disassembly at transcribing regions during RNAPII transcription. Mutants, resulting in reduced nucleosome-barrier, such as deletion mutants of histones H3/H4 themselves and the genes encoding components of histone deacetylase Clr6 complex II suppress the defects in growth and RNAPII occupancy of cells lacking Fun30Fft3. These data suggest that RNAPII utilizes the chromatin remodeller, Fun30Fft3, to overcome the nucleosome barrier to transcription elongation.

SUBMITTER: Lee J 

PROVIDER: S-EPMC5321744 | biostudies-literature | 2017 Feb

REPOSITORIES: biostudies-literature

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Chromatin remodeller Fun30<sup>Fft3</sup> induces nucleosome disassembly to facilitate RNA polymerase II elongation.

Lee Junwoo J   Choi Eun Shik ES   Seo Hogyu David HD   Kang Keunsoo K   Gilmore Joshua M JM   Florens Laurence L   Washburn Michael P MP   Choe Joonho J   Workman Jerry L JL   Lee Daeyoup D  

Nature communications 20170220


Previous studies have revealed that nucleosomes impede elongation of RNA polymerase II (RNAPII). Recent observations suggest a role for ATP-dependent chromatin remodellers in modulating this process, but direct in vivo evidence for this is unknown. Here using fission yeast, we identify Fun30<sup>Fft3</sup> as a chromatin remodeller, which localizes at transcribing regions to promote RNAPII transcription. Fun30<sup>Fft3</sup> associates with RNAPII and collaborates with the histone chaperone, FAC  ...[more]

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