Literature DB >> 26534951

Divergent Residues Within Histone H3 Dictate a Unique Chromatin Structure in Saccharomyces cerevisiae.

Kristina L McBurney1, Andrew Leung2, Jennifer K Choi1, Benjamin J E Martin1, Nicholas A T Irwin1, Till Bartke3, Christopher J Nelson2, LeAnn J Howe4.   

Abstract

Histones are among the most conserved proteins known, but organismal differences do exist. In this study, we examined the contribution that divergent amino acids within histone H3 make to cell growth and chromatin structure in Saccharomyces cerevisiae. We show that, while amino acids that define histone H3.3 are dispensable for yeast growth, substitution of residues within the histone H3 α3 helix with human counterparts results in a severe growth defect. Mutations within this domain also result in altered nucleosome positioning, both in vivo and in vitro, which is accompanied by increased preference for nucleosome-favoring sequences. These results suggest that divergent amino acids within the histone H3 α3 helix play organismal roles in defining chromatin structure.
Copyright © 2016 by the Genetics Society of America.

Entities:  

Keywords:  H3; S. cerevisiae; histone; nucleosome positioning

Mesh:

Substances:

Year:  2015        PMID: 26534951      PMCID: PMC4701097          DOI: 10.1534/genetics.115.180810

Source DB:  PubMed          Journal:  Genetics        ISSN: 0016-6731            Impact factor:   4.562


  44 in total

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