Identification of a new class of protein kinases represented by eukaryotic elongation factor-2 kinase Journal Article


Authors: Ryazanov, A. G.; Ward, M. D.; Mendola, C. E.; Pavur, K. S.; Dorovkov, M. V.; Wiedmann, M.; Erdjument-Bromage, H.; Tempst, P.; Parmer, T. G.; Prostko, C. R.; Germino, F. J.; Hait, W. N.
Article Title: Identification of a new class of protein kinases represented by eukaryotic elongation factor-2 kinase
Abstract: The several hundred members of the eukaryotic protein kinase superfamily characterized to date share a similar catalytic domain structure, consisting of 12 conserved subdomains. Here we report the existence and wide occurrence in eukaryotes of a protein kinase with a completely different structure. We cloned and sequenced the human, mouse, rat, and Caenorhabditis elegans eukaryotic elongation factor-2 kinase (eEF-2 kinase) and found that with the exception of the ATP-binding site, they do not contain any sequence motifs characteristic of the eukaryotic protein kinase superfamily. Comparison of different eEF-2 kinase sequences reveals a highly conserved region of ≃200 amino acids which was found to be homologous to the catalytic domain of the recently described myosin heavy chain kinase A (MHCK A) from Dictyostelium. This suggests that eEF-2 kinase and MHCK A are members of a new class of protein kinases with a novel catalytic domain structure.
Keywords: gene sequence; sequence analysis; polymerase chain reaction; animals; mice; transcription, genetic; molecular cloning; cloning, molecular; amino acid sequence; conserved sequence; molecular sequence data; sequence homology, amino acid; enzyme analysis; recombinant proteins; protein biosynthesis; base sequence; binding sites; rats; caenorhabditis elegans; dna primers; adenosine triphosphate; sequence homology; enzyme structure; dictyostelium; enzyme active site; rabbits; myosin heavy chain; ca(2+)-calmodulin dependent protein kinase; enzyme isolation; reticulocytes; humans; priority journal; article; elongation factor 2; sarcodina
Journal Title: Proceedings of the National Academy of Sciences of the United States of America
Volume: 94
Issue: 10
ISSN: 0027-8424
Publisher: National Academy of Sciences  
Date Published: 1997-05-13
Start Page: 4884
End Page: 4889
Language: English
DOI: 10.1073/pnas.94.10.4884
PUBMED: 9144159
PROVIDER: scopus
PMCID: PMC24600
DOI/URL:
Notes: Article -- Export Date: 17 March 2017 -- Source: Scopus
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  1. Paul J Tempst
    324 Tempst