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 |