UMMS Affiliation
Department of Molecular, Cell, and Cancer Biology
Publication Date
2016-04-30
Document Type
Article
Disciplines
Biochemistry | Cell Biology | Genetics and Genomics | Molecular Biology
Abstract
BACKGROUND: Nucleosomes have an important role in modulating access of DNA by regulatory factors. The role specific histone residues have in this process has been shown to be an important mechanism of transcription regulation. Previously, we identified eight amino acids in histones H3 and H4 that are required for nucleosome occupancy over highly transcribed regions of the genome.
RESULTS: We investigate the mechanism through which three of these previously identified histone H3 amino acids regulate nucleosome architecture. We find that histone H3 K122, Q120, and R49 are required for Spt2, Spt6, and Spt16 occupancies at genomic locations where transcription rates are high, but not over regions of low transcription rates. Furthermore, substitution at one residue, K122, located on the dyad axis of the nucleosome, results in improper reassembly and disassembly of nucleosomes, likely accounting for the transcription rate-dependent regulation by these mutant histones.
CONCLUSIONS: These data show that when specific amino acids of histone proteins are substituted, Spt2, Spt6, and Spt16 occupancies are reduced and nucleosome dynamics are altered. Therefore, these data support a mechanism for histone chaperone binding where these factors interact with histone proteins to promote their activities during transcription.
Keywords
Chromatin, Histone H3 K122, Histone chaperone, SRG1/SER3, Saccharomyces cerevisiae, Spt16, Spt2, Spt6, Transcription
DOI of Published Version
10.1186/s13072-016-0066-4
Source
Epigenetics Chromatin. 2016 Apr 30;9:17. doi: 10.1186/s13072-016-0066-4. eCollection 2016. Link to article on publisher's site
Journal/Book/Conference Title
Epigenetics and chromatin
Related Resources
PubMed ID
27134679
Repository Citation
Hainer SJ, Martens JA. (2016). Regulation of chaperone binding and nucleosome dynamics by key residues within the globular domain of histone H3. Open Access Articles. https://doi.org/10.1186/s13072-016-0066-4. Retrieved from https://escholarship.umassmed.edu/oapubs/2895
Creative Commons License
This work is licensed under a Creative Commons Attribution 4.0 License.
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