Yeast histone H2A and H2B amino termini have interchangeable functions - PubMed (original) (raw)
Yeast histone H2A and H2B amino termini have interchangeable functions
T Schuster et al. Cell. 1986.
Abstract
The N-terminal ends of histones H2B and H2A have very different sequences and rates of evolution. However, they both extend from the nucleosome core and are positively charged. Short sequences at the C termini of both proteins also differ from each other and appear to be hydrophilic. Deletions at the N and C termini of yeast histones H2B2 and H2A1 do not obviously affect the cell's viability under normal growth conditions. However, deletions at the N termini of both H2B and H2A in the same cell are lethal or result in greatly reduced viability. Even switching portions of the N termini between H2B and H2A to create two chimeric histone proteins within the same cell has no obvious effect on viability. This supports the argument that the N-terminal end of one protein complements the function of the other.
Similar articles
- Histone H2A subtypes associate interchangeably in vivo with histone H2B subtypes.
Kolodrubetz D, Rykowski MC, Grunstein M. Kolodrubetz D, et al. Proc Natl Acad Sci U S A. 1982 Dec;79(24):7814-8. doi: 10.1073/pnas.79.24.7814. Proc Natl Acad Sci U S A. 1982. PMID: 6760203 Free PMC article. - Yeast histone H2B containing large amino terminus deletions can function in vivo.
Wallis JW, Rykowski M, Grunstein M. Wallis JW, et al. Cell. 1983 Dec;35(3 Pt 2):711-9. doi: 10.1016/0092-8674(83)90104-6. Cell. 1983. PMID: 6360379 - Residues in the Nucleosome Acidic Patch Regulate Histone Occupancy and Are Important for FACT Binding in Saccharomyces cerevisiae.
Hodges AJ, Gloss LM, Wyrick JJ. Hodges AJ, et al. Genetics. 2017 Jul;206(3):1339-1348. doi: 10.1534/genetics.117.201939. Epub 2017 May 3. Genetics. 2017. PMID: 28468903 Free PMC article. - The role of histone H2A and H2B post-translational modifications in transcription: a genomic perspective.
Wyrick JJ, Parra MA. Wyrick JJ, et al. Biochim Biophys Acta. 2009 Jan;1789(1):37-44. doi: 10.1016/j.bbagrm.2008.07.001. Epub 2008 Jul 14. Biochim Biophys Acta. 2009. PMID: 18675384 Review. - [Structure and function of histone chaperone FACT].
Bondarenko MT, Maluchenko NV, Valieva ME, Gerasimova NS, Kulaeva OI, Georgiev PG, Studitsky VM. Bondarenko MT, et al. Mol Biol (Mosk). 2015 Nov-Dec;49(6):891-904. doi: 10.7868/S0026898415060026. Mol Biol (Mosk). 2015. PMID: 26710768 Review. Russian.
Cited by
- Direct assessment of histone function using histone replacement.
Corcoran ET, Jacob Y. Corcoran ET, et al. Trends Biochem Sci. 2023 Jan;48(1):53-70. doi: 10.1016/j.tibs.2022.06.010. Epub 2022 Jul 16. Trends Biochem Sci. 2023. PMID: 35853806 Free PMC article. Review. - Localization of Drosophila CENP-A to non-centromeric sites depends on the NuRD complex.
Demirdizen E, Spiller-Becker M, Förtsch A, Wilhelm A, Corless S, Bade D, Bergner A, Hessling B, Erhardt S. Demirdizen E, et al. Nucleic Acids Res. 2019 Dec 16;47(22):11589-11608. doi: 10.1093/nar/gkz962. Nucleic Acids Res. 2019. PMID: 31713634 Free PMC article. - Nucleosomes Regulate Base Excision Repair in Chromatin.
Meas R, Wyrick JJ, Smerdon MJ. Meas R, et al. Mutat Res Rev Mutat Res. 2019 Apr-Jun;780:29-36. doi: 10.1016/j.mrrev.2017.10.002. Epub 2017 Nov 7. Mutat Res Rev Mutat Res. 2019. PMID: 31388331 Free PMC article. Review. - Histones H3 and H4 require their relevant amino-tails for efficient nuclear import and replication-coupled chromatin assembly in vivo.
Ejlassi A, Menil-Philippot V, Galvani A, Thiriet C. Ejlassi A, et al. Sci Rep. 2017 Jun 8;7(1):3050. doi: 10.1038/s41598-017-03218-6. Sci Rep. 2017. PMID: 28596587 Free PMC article. - The amino-terminal tails of histones H2A and H3 coordinate efficient base excision repair, DNA damage signaling and postreplication repair in Saccharomyces cerevisiae.
Meas R, Smerdon MJ, Wyrick JJ. Meas R, et al. Nucleic Acids Res. 2015 May 26;43(10):4990-5001. doi: 10.1093/nar/gkv372. Epub 2015 Apr 20. Nucleic Acids Res. 2015. PMID: 25897129 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Molecular Biology Databases