IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v1y2010i1d10.1038_ncomms1044.html
   My bibliography  Save this article

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

Author

Listed:
  • Roberta Magnani

    (Plant Physiology/Biochemistry/Molecular Biology Program, University of Kentucky)

  • Lynnette M.A. Dirk

    (Plant Physiology/Biochemistry/Molecular Biology Program, University of Kentucky)

  • Raymond C. Trievel

    (University of Michigan Medical School)

  • Robert L. Houtz

    (Plant Physiology/Biochemistry/Molecular Biology Program, University of Kentucky)

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.

Suggested Citation

  • Roberta Magnani & Lynnette M.A. Dirk & Raymond C. Trievel & Robert L. Houtz, 2010. "Calmodulin methyltransferase is an evolutionarily conserved enzyme that trimethylates Lys-115 in calmodulin," Nature Communications, Nature, vol. 1(1), pages 1-6, December.
    • Handle: RePEc:nat:natcom:v:1:y:2010:i:1:d:10.1038_ncomms1044
    DOI: 10.1038/ncomms1044
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/ncomms1044
    File Function: Abstract
    Download Restriction: no
    File URL: https://libkey.io/10.1038/ncomms1044?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:natcom:v:1:y:2010:i:1:d:10.1038_ncomms1044. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    We have no bibliographic references for this item. You can help adding them by using this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.