Journal
BIOCHEMISTRY
Volume 51, Issue 30, Pages 5942-5950Publisher
AMER CHEMICAL SOC
DOI: 10.1021/bi300278f
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Funding
- National Institutes of Health [GM50526, GM 037537, CA158009, GM053163]
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N-Terminal methylation of free alpha-amino groups is a post-translational modification of proteins that was first described 30 years ago but has been studied very little. In this modification, the initiating M residue is cleaved and the exposed alpha-amino group is mono-, di-, or trimethylated by NRMT, a recently identified N-terminal methyltransferase. Currently, all known eukaryotic alpha-amino-methylated proteins have a unique N-terminal motif; M-X-P-K, where X is A, P, or S. NRMT can also methylate artificial substrates in vitro in which X is G, F, Y, C, M, K, R, N, Q or H. Methylation efficiencies of N-terminal amino acids are variable with respect to the identity of X. Here we use in vitro peptide methylation assays and substrate immunoprecipitations to show that the canonical M-X-P-K methylation motif is not the only one recognized by NRMT. We predict that N-terminal methylation is a widespread post-translational modification and that there is interplay between N-terminal acetylation and N-terminal methylation. We also use isothermal calorimetry experiments to demonstrate that NRMT can efficiently recognize products.
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