PMID:23086207

Citation	Chu, Y, Zhang, Z, Wang, Q, Luo, Y and Huang, L' (2012) Identification and characterization of a highly conserved crenarchaeal protein lysine methyltransferase with broad substrate specificity. J. Bacteriol. '
Abstract	Protein lysine methylation occurs extensively in crenarchaea, a major kingdom in the Archaea. However, the enzymes responsible for this type of post-translational modification have not been found. Here we report the identification and characterization of the first crenarchaeal protein lysine methyltransferase, designated aKMT, from the hyperthermophilic crenarchaeon Sulfolobus islandicus. The enzyme was capable of transferring methyl groups to selected lysine residues in a substrate protein using S-adenosyl-L-methionine (SAM) as the methyl donor. aKMT, a non-SET-domain protein, is highly conserved among crenarchaea, and distantly-related homologs also exist in the Bacteria and the Eukarya. aKMT was active over a wide range of temperature from ∼25 to 90 °C with an optimal temperature at ∼60-70 °C. Amino acid residues Y9 and T12 at the N-terminus appear to be the key residues in the putative active site of aKMT, as indicated by sequence conservation and site-directed mutagenesis. Although aKMT was identified based on its methylating activity on Cren7, the crenarchaeal chromatin protein, it exhibited broad substrate specificity and was capable of methylating a number of recombinant Sulfolobus proteins overproduced in E. coli. The finding of aKMT will help elucidate mechanisms underlining extensive protein lysine methylation and the functional significance of the post-translational protein methylation in crenarchaea.
Links	PubMed Online version:10.1128/JB.01535-12
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Annotations

Gene product	Qualifier	GO Term	Evidence Code	with/from	Aspect	Extension	Notes	Status
SULIR:KMT		GO:0016279: protein-lysine N-methyltransferase activity	ECO:0000314:		F		Fig 1D&E, Fig 2	complete CACAO 5647
SULIR:KMT	enables	GO:0016279: protein-lysine N-methyltransferase activity	ECO:0000314: direct assay evidence used in manual assertion		F		Seeded From UniProt	complete

References

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