Defining biological and biochemical functions of noncanonical SET domain proteins
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Date
2023-10-19
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Citation of Original Publication
Sun, 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.
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Access to this item will begin on 10-19-2024.
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Attribution-NonCommercial-NoDerivs 4.0 International (CC BY-NC-ND 4.0 DEED)
This 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.
Attribution-NonCommercial-NoDerivs 4.0 International (CC BY-NC-ND 4.0 DEED)
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Abstract
Within 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.