Abstract:
:Recent evidence supports the presence of an L-glutamyl methyltransferase(s) in eukaryotic cells, but this enzyme class has been defined only in certain prokaryotic species. Here, we characterize the human C6orf211 gene product as "acidic residue methyltransferase-1" (Armt1), an enzyme that specifically targets proliferating cell nuclear antigen (PCNA) in breast cancer cells, predominately methylating glutamate side chains. Armt1 homologs share structural similarities with the SAM-dependent methyltransferases, and negative regulation of activity by automethylation indicates a means for cellular control. Notably, shRNA-based knockdown of Armt1 expression in two breast cancer cell lines altered survival in response to genotoxic stress. Increased sensitivity to UV, adriamycin, and MMS was observed in SK-Br-3 cells, while in contrast, increased resistance to these agents was observed in MCF7 cells. Together, these results lay the foundation for defining the mechanism by which this post-translational modification operates in the DNA damage response (DDR).
journal_name
Cell Repjournal_title
Cell reportsauthors
Perry JJ,Ballard GD,Albert AE,Dobrolecki LE,Malkas LH,Hoelz DJdoi
10.1016/j.celrep.2015.01.054subject
Has Abstractpub_date
2015-03-03 00:00:00pages
1288-96issue
8issn
2211-1247pii
S2211-1247(15)00079-0journal_volume
10pub_type
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