The interplay of histone H2B ubiquitination with budding and fission yeast heterochromatin
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Mono-ubiquitinated histone H2B (H2B-Ub) is important for chromatin regulation of transcription, chromatin assembly, and also influences heterochromatin. In this review, we discuss the effects of H2B-Ub from nucleosome to higher-order chromatin structure. We then assess what is currently known of the role of H2B-Ub in heterochromatic silencing in budding and fission yeasts (S. cerevisiae and S. pombe), which have distinct silencing mechanisms. In budding yeast, the SIR complex initiates heterochromatin assembly with the aid of a H2B-Ub deubiquitinase, Ubp10. In fission yeast, the RNAi-dependent pathway initiates heterochromatin in the context of low H2B-Ub. We examine how the different silencing machineries overcome the challenge of H2B-Ub chromatin and highlight the importance of using these microorganisms to further our understanding of H2B-Ub in heterochromatic silencing pathways.
KeywordsSIR complex Ubp10 Ubiquitination Silencing Heterochromatin Epigenetics
We would like to thank T. Yao for helpful discussions, and E. Duncan and R. Ancar for feedback with this manuscript. This work was supported by NIH Grants T32GM008730 (A. Z.) and R35GM119575 (A. M. J).
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Conflict of interest
The authors declare that they have no conflict of interest.
- Flury V, Georgescu PR, Iesmantavicius V, Shimada Y, Kuzdere T, Braun S, Buhler M (2017) The histone acetyltransferase Mst2 protects active chromatin from epigenetic silencing by acetylating the ubiquitin ligase Brl1. Mol Cell 67:294.e299–307.e299. https://doi.org/10.1016/j.molcel.2017.05.026 CrossRefGoogle Scholar
- Kouranti I, McLean JR, Feoktistova A, Liang P, Johnson AE, Roberts-Galbraith RH, Gould KL (2010) A global census of fission yeast deubiquitinating enzyme localization and interaction networks reveals distinct compartmentalization profiles and overlapping functions in endocytosis and polarity. PLoS Biol. https://doi.org/10.1371/journal.pbio.1000471 PubMedPubMedCentralCrossRefGoogle Scholar
- Kueng S, Oppikofer M, Gasser SM (2013) SIR proteins and the assembly of silent chromatin in budding yeast. Annu Rev Genet 47:275–306. https://doi.org/10.1146/annurev-genet-021313-173730 CrossRefPubMedGoogle Scholar
- Ng HH, Ciccone DN, Morshead KB, Oettinger MA, Struhl K (2003a) Lysine-79 of histone H3 is hypomethylated at silenced loci in yeast and mammalian cells: a potential mechanism for position-effect variegation. Proc Natl Acad Sci USA 100:1820–1825. https://doi.org/10.1073/pnas.0437846100 CrossRefPubMedGoogle Scholar
- Suganuma T, Workman JL (2011) Signals and combinatorial functions of histone modifications. Annu Rev Biochem 80:473–499. https://doi.org/10.1146/annurev-biochem-061809-175347 CrossRefPubMedGoogle Scholar
- Wood A, Schneider J, Dover J, Johnston M, Shilatifard A (2003) The Paf1 complex is essential for histone monoubiquitination by the Rad6–Bre1 complex, which signals for histone methylation by COMPASS and Dot1p. J Biol Chem 278:34739–34742. https://doi.org/10.1074/jbc.C300269200 CrossRefPubMedGoogle Scholar