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From Proteopedia
Crystal structure of the RRM domain of human SETD1B
Structural highlights
FunctionSET1B_HUMAN Histone methyltransferase that specifically methylates 'Lys-4' of histone H3, when part of the SET1 histone methyltransferase (HMT) complex, but not if the neighboring 'Lys-9' residue is already methylated. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. The non-overalpping localization with SETD1A suggests that SETD1A and SETD1B make non-redundant contributions to the epigenetic control of chromatin structure and gene expression. Specifically tri-methylates 'Lys-4' of histone H3 in vitro. Publication Abstract from PubMedSETD1A and SETD1B originate from Set1, the sole H3K4 methyltransferase in yeast, and they play important roles in active gene transcription. Here, we present the crystal structures of the RRM domains of human SETD1A and SETD1B. Although both RRM domains adopt a canonical RRM fold, their structural features are different from that of the yeast Set1 RRM domain, their yeast homolog. By using an ITC binding assay, we found an intrinsically disordered region in SETD1A/B binds WDR82. The structural analysis implies that the positively charged regions within human RRM domains might be involved in binding to RNA. Our work provides structural insight into the assembly of WDR82 with the catalytic subunits SETD1A/B in the context of the whole complex. Molecular insight into the SETD1A/B N-terminal region and its interaction with WDR82.,Bao S, Xu C Biochem Biophys Res Commun. 2023 May 28;658:136-140. doi: , 10.1016/j.bbrc.2023.03.064. Epub 2023 Mar 31. PMID:37030068[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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