Matches in SemOpenAlex for { <https://semopenalex.org/work/W2040139524> ?p ?o ?g. }
Showing items 1 to 80 of
80
with 100 items per page.
- W2040139524 endingPage "16364" @default.
- W2040139524 startingPage "16351" @default.
- W2040139524 abstract "A high level of the post-translational modification, acetylation, is found on the N-terminal regions of the core histones H2A, H2B, H3, and H4 and is primarily located in the nucleosomes of active genes. An in vitro transcription system was applied, which utilizes T7 RNA polymerase and template DNAs that are either moderately or highly positively coiled, to determine whether acetylation alters the dynamics of histone displacement from these templates during transcription. To measure displacement, an excess of a competitor (negatively coiled DNA reconstituted with unlabeled H3−H4) was included during the transcription process. Acetylated but not unacetylated 3H-labeled H3−H4 was found to displace with high frequency from the moderately positively coiled template. This displacement of acetylated H3−H4 was not observed when the template was highly positively coiled. Acetylated 3H-labeled H2A−H2B also preferentially displaced to the competitor, but in this instance, transcription-induced stress on the highly positively coiled template was required. The histone chaperone, NAP1, was found to facilitate the displacement of both H3−H4 and H2A−H2B. Surprisingly, when acetylated H2A−H2B and acetylated H3−H4 were reconstituted together in the same nucleosomes, the displacement of acetylated H2A−H2B was much reduced during transcription. We conclude that acetylation alters nucleosome stability by enhancing displacement of H3−H4, while decreasing the displacement of H2A−H2B. These results are discussed with regard to potential in vivo conditions in which these observations may be relevant." @default.
- W2040139524 created "2016-06-24" @default.
- W2040139524 creator A5002206077 @default.
- W2040139524 creator A5081365529 @default.
- W2040139524 date "2005-11-11" @default.
- W2040139524 modified "2023-09-27" @default.
- W2040139524 title "Histone Release during Transcription: Acetylation Stabilizes the Interaction of the H2A−H2B Dimer with the H3−H4 Tetramer in Nucleosomes That Are on Highly Positively Coiled DNA" @default.
- W2040139524 cites W2047534579 @default.
- W2040139524 cites W2106161842 @default.
- W2040139524 doi "https://doi.org/10.1021/bi050876o" @default.
- W2040139524 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/16331996" @default.
- W2040139524 hasPublicationYear "2005" @default.
- W2040139524 type Work @default.
- W2040139524 sameAs 2040139524 @default.
- W2040139524 citedByCount "11" @default.
- W2040139524 countsByYear W20401395242014 @default.
- W2040139524 countsByYear W20401395242015 @default.
- W2040139524 countsByYear W20401395242017 @default.
- W2040139524 countsByYear W20401395242018 @default.
- W2040139524 crossrefType "journal-article" @default.
- W2040139524 hasAuthorship W2040139524A5002206077 @default.
- W2040139524 hasAuthorship W2040139524A5081365529 @default.
- W2040139524 hasConcept C101762097 @default.
- W2040139524 hasConcept C104317684 @default.
- W2040139524 hasConcept C119157956 @default.
- W2040139524 hasConcept C12554922 @default.
- W2040139524 hasConcept C138885662 @default.
- W2040139524 hasConcept C150194340 @default.
- W2040139524 hasConcept C179926584 @default.
- W2040139524 hasConcept C185592680 @default.
- W2040139524 hasConcept C2776745794 @default.
- W2040139524 hasConcept C2779085176 @default.
- W2040139524 hasConcept C41895202 @default.
- W2040139524 hasConcept C552990157 @default.
- W2040139524 hasConcept C55493867 @default.
- W2040139524 hasConcept C64350747 @default.
- W2040139524 hasConcept C64927066 @default.
- W2040139524 hasConcept C84772758 @default.
- W2040139524 hasConcept C86803240 @default.
- W2040139524 hasConcept C95444343 @default.
- W2040139524 hasConceptScore W2040139524C101762097 @default.
- W2040139524 hasConceptScore W2040139524C104317684 @default.
- W2040139524 hasConceptScore W2040139524C119157956 @default.
- W2040139524 hasConceptScore W2040139524C12554922 @default.
- W2040139524 hasConceptScore W2040139524C138885662 @default.
- W2040139524 hasConceptScore W2040139524C150194340 @default.
- W2040139524 hasConceptScore W2040139524C179926584 @default.
- W2040139524 hasConceptScore W2040139524C185592680 @default.
- W2040139524 hasConceptScore W2040139524C2776745794 @default.
- W2040139524 hasConceptScore W2040139524C2779085176 @default.
- W2040139524 hasConceptScore W2040139524C41895202 @default.
- W2040139524 hasConceptScore W2040139524C552990157 @default.
- W2040139524 hasConceptScore W2040139524C55493867 @default.
- W2040139524 hasConceptScore W2040139524C64350747 @default.
- W2040139524 hasConceptScore W2040139524C64927066 @default.
- W2040139524 hasConceptScore W2040139524C84772758 @default.
- W2040139524 hasConceptScore W2040139524C86803240 @default.
- W2040139524 hasConceptScore W2040139524C95444343 @default.
- W2040139524 hasIssue "49" @default.
- W2040139524 hasLocation W20401395241 @default.
- W2040139524 hasLocation W20401395242 @default.
- W2040139524 hasOpenAccess W2040139524 @default.
- W2040139524 hasPrimaryLocation W20401395241 @default.
- W2040139524 hasRelatedWork W1975210846 @default.
- W2040139524 hasRelatedWork W2011783533 @default.
- W2040139524 hasRelatedWork W2040139524 @default.
- W2040139524 hasRelatedWork W2068768766 @default.
- W2040139524 hasRelatedWork W2069179692 @default.
- W2040139524 hasRelatedWork W2111089783 @default.
- W2040139524 hasRelatedWork W2130830586 @default.
- W2040139524 hasRelatedWork W2327710626 @default.
- W2040139524 hasRelatedWork W4249198188 @default.
- W2040139524 hasRelatedWork W4283119350 @default.
- W2040139524 hasVolume "44" @default.
- W2040139524 isParatext "false" @default.
- W2040139524 isRetracted "false" @default.
- W2040139524 magId "2040139524" @default.
- W2040139524 workType "article" @default.