Journal
CELL REPORTS
Volume 10, Issue 8, Pages 1288-1296Publisher
CELL PRESS
DOI: 10.1016/j.celrep.2015.01.054
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Funding
- Eastern Maine Healthcare Systems
- Maine Cancer Foundation Grant
- DOD BCRP [DAMD17-02-1-0467, DAMD17-99-1-9273]
- USAMRMC [W81XWH-10-2-0014]
- NIH [5R01CA121289-03, AR059968-03]
- Sue and Joe Cyr from Old Town, ME
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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).
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