Molecular cloning of a novel protein containing the association domain of calmodulin-dependent protein kinase II

Journal of Biochemistry
R SugaiH Fujisawa

Abstract

The cDNA of a novel protein, which contains the association domain of alpha isoform of calmodulin-dependent protein kinase II (CaM-kinase II alpha), was cloned from rat skeletal muscle. This protein, called alpha KAP, consisted of 200 amino acid residues with a molecular weight of 22,583. alpha KAP has a highly hydrophobic amino-terminal stretch of 25 amino acids which is absent from CaM-kinase II alpha, suggesting that this protein is either a secretory protein or an integral membrane protein. Northern blot analysis with a probe specific for alpha KAP detected three distinct mRNA species of 4.0, 2.4, and 1.5 kb in rat skeletal muscle. The 4.0- and 2.4-kb RNAs were also detected in heart, and at much lower levels in lung, kidney, and testis. Western blot analysis, using antibody raised against a synthetic peptide corresponding to the carboxyl-terminal 15 amino acids, revealed a single band corresponding in mobility to a molecular weight of 21,000 in crude extracts of both rat skeletal muscle and bacteria transformed with the cDNA, suggesting that no significant post-translational modification, such as excision of the amino-terminal hydrophobic segment, occurred. This, together with the fact that alpha KAP was recovered in the h...Continue Reading

Citations

Feb 21, 2003·Biochemical and Biophysical Research Communications·Ernesto DamianiAlfredo Margreth
Nov 15, 2006·Developmental Dynamics : an Official Publication of the American Association of Anatomists·Sarah C RothschildRobert M Tombes
Sep 21, 2002·Molecular and Cellular Biology·Thomas F WestbrookDennis J McCance
Mar 18, 2003·Molecular and Cellular Biology·Sébastien JeayGail E Sonenshein
Nov 19, 2004·Journal of Muscle Research and Cell Motility·Roberta SacchettoAlfredo Margreth
May 6, 2009·Neurochemical Research·Kathryn A Skelding, John A P Rostas

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