Cloning and expression of cDNA encoding protein synthesis elongation factor-2 kinase

Redpath, N.T. and Price, Nigel T. and Proud, Christopher G. (1996) Cloning and expression of cDNA encoding protein synthesis elongation factor-2 kinase. Journal of Biological Chemistry, 271 (29). pp. 17547-17554. ISSN 0021-9258. (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided)

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A cDNA from rat skeletal muscle encoding calcium/calmodulin-dependent eukaryotic elongation factor-2 kinase (eEF-2K) has been cloned and sequenced, and the amino acid sequence of the protein has been deduced. The kinase is composed of 724 amino acids and has a predicted molecular mass of 81,499 Da. The cDNA was judged to be full-length, as the protein, expressed in rabbit reticulocyte lysate or wheat germ extract, migrated upon SDS-PAGE with the same apparent molecular weight as the purified kinase and possessed eEF-2K activity, eEF-2K contains all of the 12 catalytic subdomains present in the majority of protein kinases, but they are atypical and display only limited homology with other kinases. A putative calmodulin-binding domain is present C-terminal to the catalytic domain as is a putative pseudosubstrate sequence. Two antipeptide antibodies raised against sequences derived from a partial rabbit cDNA clone, cross-reacted with purified eEF-2K, and one also immunoprecipitated eEF-2K activity from cell extracts. Northern blot analysis demonstrated that eEF-2K mRNA is expressed in a number of different tissues and that it may exist in multiple forms.

Item Type: Article
Subjects: Q Science > QD Chemistry
Q Science > QP Physiology (Living systems) > QP506 Molecular biology
Divisions: Faculties > Science Technology and Medical Studies > School of Biosciences
Depositing User: F.D. Zabet
Date Deposited: 08 May 2009 15:22
Last Modified: 16 Jul 2014 14:06
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