Abstract:
:Set8 is the only mammalian monomethyltransferase responsible for H4K20me1, a methyl mark critical for genomic integrity of eukaryotic cells. We present here a structural model for how Set8 uses multivalent interactions to bind and methylate the nucleosome based on crystallographic and solution studies of the Set8/nucleosome complex. Our studies indicate that Set8 employs its i-SET and c-SET domains to engage nucleosomal DNA 1 to 1.5 turns from the nucleosomal dyad and in doing so, it positions the SET domain for catalysis with H4 Lys20. Surprisingly, we find that a basic N-terminal extension to the SET domain plays an even more prominent role in nucleosome binding, possibly by making an arginine anchor interaction with the nucleosome H2A/H2B acidic patch. We further show that proliferating cell nuclear antigen and the nucleosome compete for binding to Set8 through this basic extension, suggesting a mechanism for how nucleosome binding protects Set8 from proliferating cell nuclear antigen-dependent degradation during the cell cycle.
journal_name
J Mol Bioljournal_title
Journal of molecular biologyauthors
Girish TS,McGinty RK,Tan Sdoi
10.1016/j.jmb.2016.02.025subject
Has Abstractpub_date
2016-04-24 00:00:00pages
1531-43issue
8eissn
0022-2836issn
1089-8638pii
S0022-2836(16)00155-8journal_volume
428pub_type
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