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TitleCryo-EM and biochemical analyses of the nucleosome containing the human histone H3 variant H3.8.
Journal, issue, pagesJ Biochem, Vol. 174, Issue 6, Page 549-559, Year 2023
Publish dateNov 30, 2023
AuthorsSeiya Hirai / Tomoya Kujirai / Munetaka Akatsu / Mitsuo Ogasawara / Haruhiko Ehara / Shun-Ichi Sekine / Yasuyuki Ohkawa / Yoshimasa Takizawa / Hitoshi Kurumizaka /
PubMed AbstractHistone H3.8 is a non-allelic human histone H3 variant derived from H3.3. H3.8 reportedly forms an unstable nucleosome, but its structure and biochemical characteristics have not been revealed yet. ...Histone H3.8 is a non-allelic human histone H3 variant derived from H3.3. H3.8 reportedly forms an unstable nucleosome, but its structure and biochemical characteristics have not been revealed yet. In the present study, we reconstituted the nucleosome containing H3.8. Consistent with previous results, the H3.8 nucleosome is thermally unstable as compared to the H3.3 nucleosome. The entry/exit DNA regions of the H3.8 nucleosome are more accessible to micrococcal nuclease than those of the H3.3 nucleosome. Nucleosome transcription assays revealed that the RNA polymerase II (RNAPII) pausing around the superhelical location (SHL) -1 position, which is about 60 base pairs from the nucleosomal DNA entry site, is drastically alleviated. On the other hand, the RNAPII pausing around the SHL(-5) position, which is about 20 base pairs from the nucleosomal DNA entry site, is substantially increased. The cryo-electron microscopy structure of the H3.8 nucleosome explains the mechanisms of the enhanced accessibility of the entry/exit DNA regions, reduced thermal stability and altered RNAPII transcription profile.
External linksJ Biochem / PubMed:37757444 / PubMed Central
MethodsEM (single particle)
Resolution2.26133 Å
Structure data

37070

8kb5

EMDB-37070, PDB-8kb5:
Cryo-EM structure of the human nucleosome containing H3.8
Method: EM (single particle) / Resolution: 2.26133 Å

Source
  • homo sapiens (human)
  • synthetic construct (others)
KeywordsDNA BINDING PROTEIN / complex / chromatin / nucleosome / gene regulation

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