Defining biological and biochemical functions of noncanonical SET domain proteins

dc.contributor.authorSun, Winny
dc.contributor.authorJustice, Isabella
dc.contributor.authorGreen, Erin
dc.date.accessioned2023-11-08T13:59:43Z
dc.date.available2023-11-08T13:59:43Z
dc.date.issued2023-10-19
dc.description.abstractWithin the SET domain superfamily of lysine methyltransferases, there is a well-conserved subfamily, frequently referred to as the Set3 SET domain subfamily, which contain noncanonical SET domains carrying divergent amino acid sequences. These proteins are implicated in diverse biological processes including stress responses, cell differentiation, and development, and their disruption is linked to diseases including cancer and neurodevelopmental disorders. Interestingly, biochemical and structural analysis indicates that they do not possess catalytic methyltransferase activity. At the molecular level, Set3 SET domain proteins appear to play critical roles in the regulation of gene expression, particularly repression and heterochromatin maintenance, and in some cases, via scaffolding other histone modifying activities at chromatin. Here, we explore the common and unique functions among Set3 SET domain subfamily proteins and analyze what is known about the specific contribution of the conserved SET domain to functional roles of these proteins, as well as propose areas of investigation to improve understanding of this important, noncanonical subfamily of proteins.en_US
dc.description.sponsorshipThe authors thank members of the Green Lab for helpful discussion and acknowledge support from National Institutes of Health R01GM124342 and a UMBC START award to EMG.en_US
dc.description.urihttps://www.sciencedirect.com/science/article/pii/S0022283623004291en_US
dc.format.extent9 pagesen_US
dc.genrejournal articlesen_US
dc.genrepostprintsen_US
dc.identifierdoi:10.13016/m2gwf2-wcau
dc.identifier.citationSun, Winny, Isabella Justice, and Erin M. Green. “Defining Biological and Biochemical Functions of Noncanonical SET Domain Proteins.” Journal of Molecular Biology, October 19, 2023, 168318. https://doi.org/10.1016/j.jmb.2023.168318.en_US
dc.identifier.urihttps://doi.org/10.1016/j.jmb.2023.168318
dc.identifier.urihttp://hdl.handle.net/11603/30588
dc.language.isoen_USen_US
dc.publisherElsevieren_US
dc.relation.isAvailableAtThe University of Maryland, Baltimore County (UMBC)
dc.relation.ispartofUMBC Biological Sciences Department Collection
dc.relation.ispartofUMBC Faculty Collection
dc.relation.ispartofUMBC Student Collection
dc.rightsAccess to this item will begin on 10-19-2024.
dc.rightsThis item is likely protected under Title 17 of the U.S. Copyright Law. Unless on a Creative Commons license, for uses protected by Copyright Law, contact the copyright holder or the author.*
dc.rightsAttribution-NonCommercial-NoDerivs 4.0 International (CC BY-NC-ND 4.0 DEED)en_US
dc.rights.urihttps://creativecommons.org/licenses/by-nc-nd/4.0/*
dc.titleDefining biological and biochemical functions of noncanonical SET domain proteinsen_US
dc.typeTexten_US
dcterms.creatorhttps://orcid.org/0000-0002-2247-9951en_US
dcterms.creatorhttps://orcid.org/0000-0003-3923-6726en_US

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