Yeast histone H3 and H4 amino termini are important for nucleosome assembly in vivo and in vitro: redundant and position-independent functions in assembly but not in gene regulation - PubMed (original) (raw)
. 1996 Mar 15;10(6):686-99.
doi: 10.1101/gad.10.6.686.
Affiliations
- PMID: 8598296
- DOI: 10.1101/gad.10.6.686
Free article
Yeast histone H3 and H4 amino termini are important for nucleosome assembly in vivo and in vitro: redundant and position-independent functions in assembly but not in gene regulation
X Ling et al. Genes Dev. 1996.
Free article
Abstract
The hydrophilic amino-terminal sequences of histones H3 and H4 extend from the highly structured nucleosome core. Here we examine the importance of the amino termini and their position in the nucleosome with regard to both nucleosome assembly and gene regulation. Despite previous conclusions based on nonphysiological nucleosome reconstitution experiments, we find that the histone amino termini are important for nucleosome assembly in vivo and in vitro. Deletion of both tails, a lethal event, alters micrococcal nuclease-generated nucleosomal ladders, plasmid superhelicity in whole cells, and nucleosome assembly in cell extracts. The H3 and H4 amino-terminal tails have redundant functions in this regard because the presence of either tail allows assembly and cellular viability. Moreover, the tails need not be attached to their native carboxy-terminal core. Their exchange re-establishes both cellular viability and nucleosome assembly. In contrast, the regulation of GAL1 and the silent mating loci by the H3 and H4 tails is highly disrupted by exchange of the histone amino termini.
Similar articles
- Sin mutations of histone H3: influence on nucleosome core structure and function.
Kurumizaka H, Wolffe AP. Kurumizaka H, et al. Mol Cell Biol. 1997 Dec;17(12):6953-69. doi: 10.1128/MCB.17.12.6953. Mol Cell Biol. 1997. PMID: 9372928 Free PMC article. - Splitting of H3-H4 tetramers at transcriptionally active genes undergoing dynamic histone exchange.
Katan-Khaykovich Y, Struhl K. Katan-Khaykovich Y, et al. Proc Natl Acad Sci U S A. 2011 Jan 25;108(4):1296-301. doi: 10.1073/pnas.1018308108. Epub 2011 Jan 10. Proc Natl Acad Sci U S A. 2011. PMID: 21220302 Free PMC article. - The N-terminal domains of histones H3 and H4 are not necessary for chromatin assembly factor-1- mediated nucleosome assembly onto replicated DNA in vitro.
Shibahara K, Verreault A, Stillman B. Shibahara K, et al. Proc Natl Acad Sci U S A. 2000 Jul 5;97(14):7766-71. doi: 10.1073/pnas.97.14.7766. Proc Natl Acad Sci U S A. 2000. PMID: 10884407 Free PMC article. - Secondary structures of the core histone N-terminal tails: their role in regulating chromatin structure.
du Preez LL, Patterton HG. du Preez LL, et al. Subcell Biochem. 2013;61:37-55. doi: 10.1007/978-94-007-4525-4_2. Subcell Biochem. 2013. PMID: 23150245 Review. - Replication-Coupled Nucleosome Assembly in the Passage of Epigenetic Information and Cell Identity.
Serra-Cardona A, Zhang Z. Serra-Cardona A, et al. Trends Biochem Sci. 2018 Feb;43(2):136-148. doi: 10.1016/j.tibs.2017.12.003. Epub 2017 Dec 29. Trends Biochem Sci. 2018. PMID: 29292063 Free PMC article. Review.
Cited by
- DNA Repair in Nucleosomes: Insights from Histone Modifications and Mutants.
Selvam K, Wyrick JJ, Parra MA. Selvam K, et al. Int J Mol Sci. 2024 Apr 16;25(8):4393. doi: 10.3390/ijms25084393. Int J Mol Sci. 2024. PMID: 38673978 Free PMC article. Review. - The Role of Histone Modification in DNA Replication-Coupled Nucleosome Assembly and Cancer.
Zhang Y, Zhang Q, Zhang Y, Han J. Zhang Y, et al. Int J Mol Sci. 2023 Mar 3;24(5):4939. doi: 10.3390/ijms24054939. Int J Mol Sci. 2023. PMID: 36902370 Free PMC article. Review. - Measuring the buffering capacity of gene silencing in Saccharomyces cerevisiae.
Wu K, Dhillon N, Du K, Kamakaka RT. Wu K, et al. Proc Natl Acad Sci U S A. 2021 Dec 7;118(49):e2111841118. doi: 10.1073/pnas.2111841118. Proc Natl Acad Sci U S A. 2021. PMID: 34857629 Free PMC article. - Replication-Coupled Chromatin Remodeling: An Overview of Disassembly and Assembly of Chromatin during Replication.
Duc C, Thiriet C. Duc C, et al. Int J Mol Sci. 2021 Jan 23;22(3):1113. doi: 10.3390/ijms22031113. Int J Mol Sci. 2021. PMID: 33498649 Free PMC article. Review. - 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.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Molecular Biology Databases
Research Materials