Identification in turkey gizzard of an acidic protein related to the C-terminal portion of smooth muscle myosin light chain kinase

M. Ito, R. Dabrowska, Vincent Guerriero, D. J. Hartshorne

Research output: Contribution to journalArticle

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Abstract

The isolation of an acidic protein, pI 4.5, that is abundant in turkey gizzard is described. Its apparent molecular weight measured by electrophoretic procedures is 24,000. This protein is phosphorylated by the catalytic subunit of the cAMP-dependent protein kinase and one phosphorylation site is indicated. From sequence determinations of tryptic peptides it is concluded that this protein is closely related to the C-terminal part of smooth muscle myosin light chain kinase. The initiation site for the protein is to the C-terminal side of the calmodulin-binding site. From the sequence data an estimated molecular weight is 18,000. This protein is expressed independently, as indicated by a blocked N terminus, and is probably the translation product of the 2.7-kilobase RNA detected previously in chicken gizzard (Guerriero, V., Jr., Russo, M.A., Olson, N.J., Purtkey, J.A., and Means, A.R. (1986) Biochemistry 25, 8372-8381). Because of its putative origin as the C-terminal end of smooth muscle myosin light chain kinase, it is termed 'telokin' (from a combination of kinase and the Greek telos, 'end').

Original languageEnglish (US)
Pages (from-to)13971-13974
Number of pages4
JournalJournal of Biological Chemistry
Volume264
Issue number24
StatePublished - 1989

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Smooth Muscle Myosins
Avian Gizzard
Myosin-Light-Chain Kinase
Proteins
Molecular Weight
Molecular weight
Biochemistry
Phosphorylation
Protein Sequence Analysis
Calmodulin
Cyclic AMP-Dependent Protein Kinases
Chickens
Catalytic Domain
Phosphotransferases
Binding Sites
RNA
Peptides

ASJC Scopus subject areas

  • Biochemistry

Cite this

Identification in turkey gizzard of an acidic protein related to the C-terminal portion of smooth muscle myosin light chain kinase. / Ito, M.; Dabrowska, R.; Guerriero, Vincent; Hartshorne, D. J.

In: Journal of Biological Chemistry, Vol. 264, No. 24, 1989, p. 13971-13974.

Research output: Contribution to journalArticle

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AU - Guerriero, Vincent

AU - Hartshorne, D. J.

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N2 - The isolation of an acidic protein, pI 4.5, that is abundant in turkey gizzard is described. Its apparent molecular weight measured by electrophoretic procedures is 24,000. This protein is phosphorylated by the catalytic subunit of the cAMP-dependent protein kinase and one phosphorylation site is indicated. From sequence determinations of tryptic peptides it is concluded that this protein is closely related to the C-terminal part of smooth muscle myosin light chain kinase. The initiation site for the protein is to the C-terminal side of the calmodulin-binding site. From the sequence data an estimated molecular weight is 18,000. This protein is expressed independently, as indicated by a blocked N terminus, and is probably the translation product of the 2.7-kilobase RNA detected previously in chicken gizzard (Guerriero, V., Jr., Russo, M.A., Olson, N.J., Purtkey, J.A., and Means, A.R. (1986) Biochemistry 25, 8372-8381). Because of its putative origin as the C-terminal end of smooth muscle myosin light chain kinase, it is termed 'telokin' (from a combination of kinase and the Greek telos, 'end').

AB - The isolation of an acidic protein, pI 4.5, that is abundant in turkey gizzard is described. Its apparent molecular weight measured by electrophoretic procedures is 24,000. This protein is phosphorylated by the catalytic subunit of the cAMP-dependent protein kinase and one phosphorylation site is indicated. From sequence determinations of tryptic peptides it is concluded that this protein is closely related to the C-terminal part of smooth muscle myosin light chain kinase. The initiation site for the protein is to the C-terminal side of the calmodulin-binding site. From the sequence data an estimated molecular weight is 18,000. This protein is expressed independently, as indicated by a blocked N terminus, and is probably the translation product of the 2.7-kilobase RNA detected previously in chicken gizzard (Guerriero, V., Jr., Russo, M.A., Olson, N.J., Purtkey, J.A., and Means, A.R. (1986) Biochemistry 25, 8372-8381). Because of its putative origin as the C-terminal end of smooth muscle myosin light chain kinase, it is termed 'telokin' (from a combination of kinase and the Greek telos, 'end').

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