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PMID: 20975703 Published · epublish English Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.

Calmodulin methyltransferase is an evolutionarily conserved enzyme that trimethylates Lys-115 in calmodulin.

Nature communications ·Vol. 1 ·2010-07-27 ·Pages 43

Magnani R, Dirk LM, Trievel RC, Houtz RL

Abstract

Calmodulin (CaM) is a key mediator of calcium-dependent signalling and is subject to regulatory post-translational modifications, including trimethylation of Lys-115. In this paper, we identify a class I, non-SET domain protein methyltransferase, calmodulin-lysine N-methyltransferase (EC 2.1.1.60). A polypeptide chosen from a fraction enriched in calmodulin methyltransferase activity was trypsinized and analysed by tandem mass spectrometry. The amino-acid sequence obtained identified conserved, homologous proteins of unknown function across a wide range of species, thus implicating a broad role for lysine methylation in calcium-dependent signalling. Encoded by c2orf34, the human homologue is a component of two related multigene deletion syndromes in humans. Human, rat, frog, insect and plant homologues were cloned and Escherichia coli-recombinant proteins catalysed the formation of a trimethyllysyl residue at position 115 in CaM, as verified by product analyses and mass spectrometry.

MeSH Terms
Amino Acid Sequence Animals Calmodulin/metabolism Chromatography, Liquid Chromatography, Thin Layer Electrophoresis, Polyacrylamide Gel Humans Insect Proteins/chemistry,genetics,metabolism Lysine/metabolism Methylation Methyltransferases/chemistry,genetics,metabolism Molecular Sequence Data Plant Proteins/chemistry,genetics,metabolism Protein Processing, Post-Translational Protein Structure, Secondary Rats Sequence Homology, Amino Acid Tandem Mass Spectrometry
Chemicals
Calmodulin Insect Proteins Plant Proteins Methyltransferases calmodulin methyltransferase Lysine
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Magnani Roberta
Department of Horticulture, Plant Physiology/Biochemistry/Molecular Biology Program, University of Kentucky, Lexington, Kentucky 40546, USA.
Dirk Lynnette M A
Trievel Raymond C
Houtz Robert L
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Article Info
Journal
Nature communications
Abbr.
Nat Commun
ISSN
2041-1723
Published
2010-07-27
Epub
2010-00-27
Pages
43
Language
English
Region
England
NLM ID
101528555
Subset
IM
Grants
NCRR NIH HHS · P20 RR020171 · United States
NIGMS NIH HHS · R01 GM073839 · United States
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