Single-Molecule Imaging Reveals the Mechanism Underlying Histone Loading of Schizosaccharomyces pombe AAA plus ATPase Abo1

Cited 4 time in webofscience Cited 0 time in scopus
  • Hit : 321
  • Download : 76
DC FieldValueLanguage
dc.contributor.authorKang, Yujinko
dc.contributor.authorCho, Carolko
dc.contributor.authorLee, Kyung Sukko
dc.contributor.authorSong, Ji-Joonko
dc.contributor.authorLee, Ja Yilko
dc.date.accessioned2021-05-12T04:50:06Z-
dc.date.available2021-05-12T04:50:06Z-
dc.date.created2021-05-11-
dc.date.created2021-05-11-
dc.date.created2021-05-11-
dc.date.created2021-05-11-
dc.date.issued2021-02-
dc.identifier.citationMOLECULES AND CELLS, v.44, no.2, pp.79 - +-
dc.identifier.issn1016-8478-
dc.identifier.urihttp://hdl.handle.net/10203/283658-
dc.description.abstractChromatin dynamics is essential for maintaining genomic integrity and regulating gene expression. Conserved bromodomain-containing AAA+ ATPases play important roles in nucleosome organization as histone chaperones. Recently, the high-resolution cryo-electron microscopy structures of Schizosaccharomyces pombe Abo1 revealed that it forms a hexameric ring and undergoes a conformational change upon ATP hydrolysis. In addition, single-molecule imaging demonstrated that Abo1 loads H3-H4 histones onto DNA in an ATP hydrolysisdependent manner. However, the molecular mechanism by which Abo1 loads histones remains unknown. Here, we investigated the details concerning Abo1-mediated histone loading onto DNA and the Abo1- DNA interaction using single-molecule imaging techniques and biochemical assays. We show that Abo1 does not load H2A-H2B histones. Interestingly, Abo1 deposits multiple copies of H3-H4 histones as the DNA length increases and requires at least 80 bp DNA. Unexpectedly, Abo1 weakly binds DNA regardless of ATP, and neither histone nor DNA stimulates the ATP hydrolysis activity of Abo1. Based on our results, we propose an allosteric communication model in which the ATP hydrolysis of Abo1 changes the configuration of histones to facilitate their deposition onto DNA.-
dc.languageEnglish-
dc.publisherKOREAN SOC MOLECULAR & CELLULAR BIOLOGY-
dc.titleSingle-Molecule Imaging Reveals the Mechanism Underlying Histone Loading of Schizosaccharomyces pombe AAA plus ATPase Abo1-
dc.typeArticle-
dc.identifier.wosid000637281400001-
dc.identifier.scopusid2-s2.0-85102482163-
dc.type.rimsART-
dc.citation.volume44-
dc.citation.issue2-
dc.citation.beginningpage79-
dc.citation.endingpage+-
dc.citation.publicationnameMOLECULES AND CELLS-
dc.identifier.doi10.14348/molcells.2021.2242-
dc.identifier.kciidART002691840-
dc.contributor.localauthorCho, Carol-
dc.contributor.localauthorSong, Ji-Joon-
dc.contributor.nonIdAuthorKang, Yujin-
dc.contributor.nonIdAuthorLee, Kyung Suk-
dc.contributor.nonIdAuthorLee, Ja Yil-
dc.description.isOpenAccessY-
dc.type.journalArticleArticle-
dc.subject.keywordAuthorbromodomain-containing AAA plus ATPase-
dc.subject.keywordAuthorDNA curtain-
dc.subject.keywordAuthorhistone loading-
dc.subject.keywordAuthorsingle-molecule photobleaching-
This item is cited by other documents in WoS
⊙ Detail Information in WoSⓡ Click to see webofscience_button
⊙ Cited 4 items in WoS Click to see citing articles in records_button

qr_code

  • mendeley

    citeulike


rss_1.0 rss_2.0 atom_1.0