Diversity and functional specialization of H3K9-specific histone methyltransferases.

Autor: Koryakov DE; Lab of Molecular Cytogenetics, Institute of Molecular and Cellular Biology, Novosibirsk, Russia.
Jazyk: angličtina
Zdroj: BioEssays : news and reviews in molecular, cellular and developmental biology [Bioessays] 2024 Feb; Vol. 46 (2), pp. e2300163. Date of Electronic Publication: 2023 Dec 06.
DOI: 10.1002/bies.202300163
Abstrakt: Histone modifications play a critical role in the control over activities of the eukaryotic genome; among these chemical alterations, the methylation of lysine K9 in histone H3 (H3K9) is one of the most extensively studied. The number of enzymes capable of methylating H3K9 varies greatly across different organisms: in fission yeast, only one such methyltransferase is present, whereas in mammals, 10 are known. If there are several such enzymes, each of them must have some specific function, and they can interact with one another. Thus arises a complex system of interchangeability, "division of labor," and contacts with each other and with diverse proteins. Histone methyltransferases specialize in the number of methyl groups that they attach and have different intracellular localizations as well as different distributions on chromosomes. Each also shows distinct binding to different types of sequences and has a specific set of nonhistone substrates.
(© 2023 Wiley Periodicals LLC.)
Databáze: MEDLINE
Externí odkaz: