Amino acid sequence of the phosphorylation site of bovine cardiac myosin light chain

Thomas J. Lukas; Anne Redelfs; Wilson H. Burgess; D. Martin Watterson

doi:10.1016/0003-9861(85)90212-7

Amino acid sequence of the phosphorylation site of bovine cardiac myosin light chain

Thomas J. Lukas^*, Anne Redelfs, Wilson H. Burgess, D. Martin Watterson

^*Corresponding author for this work

Pharmacology

Research output: Contribution to journal › Article › peer-review

Abstract

Amino acid sequences of peptides containing the phosphorylation site of bovine cardiac myosin light chain (L2) were determined. The site was localized to a serine residue in the tentative amino terminus of the light chain and is homologous to phosphorylation sites in other myosin light chains. Phosphorylation of bovine cardiac light chain by chicken gizzard myosin light chain kinase was Ca²⁺-calmodulin dependent. Kinetic data gave a K_m of 107; μm and a V_max of 23.6 μmol min^-1 mg^-1. In contrast to what has been observed with smooth muscle light chains, neither the phosphorylation site fragment of the cardiac light chain nor a synthetic tetradecapeptide containing the phosphorylation site were effectively phosphorylated by the chicken gizzard kinase. Phosphorylation of cardiac myosin light chains by chicken gizzard myosin light chain kinase, therefore, requires other regions of the light chain in addition to a phosphate acceptor site.

Original language	English (US)
Pages (from-to)	664-669
Number of pages	6
Journal	Archives of biochemistry and biophysics
Volume	238
Issue number	2
DOIs	https://doi.org/10.1016/0003-9861(85)90212-7
State	Published - May 1 1985

Funding

’ Supported in part by funds from National Institutes of Health Grant GM30953. ‘To whom correspondence should be addressed. 3 On leave of absence from School of Medicine, Tulane University, New Orleans, La. 4 Current Address: Department of Cell Biology, Revlon Biotechnology Research Center, Rockville, Md. ’ Abbreviations used: PTH, phenylthiohydantoin; MLCK, myosin light chain kinase, Mops, 4-morpho-linepropanesulfonie acid; BSA, bovine serum albumin; TFA, trifluoroacetic acid; TPCK, L-l-ptosylamino-2-phenylethylchloromethyl ketone.

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology

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10.1016/0003-9861(85)90212-7

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title = "Amino acid sequence of the phosphorylation site of bovine cardiac myosin light chain",

abstract = "Amino acid sequences of peptides containing the phosphorylation site of bovine cardiac myosin light chain (L2) were determined. The site was localized to a serine residue in the tentative amino terminus of the light chain and is homologous to phosphorylation sites in other myosin light chains. Phosphorylation of bovine cardiac light chain by chicken gizzard myosin light chain kinase was Ca2+-calmodulin dependent. Kinetic data gave a Km of 107; μm and a Vmax of 23.6 μmol min-1 mg-1. In contrast to what has been observed with smooth muscle light chains, neither the phosphorylation site fragment of the cardiac light chain nor a synthetic tetradecapeptide containing the phosphorylation site were effectively phosphorylated by the chicken gizzard kinase. Phosphorylation of cardiac myosin light chains by chicken gizzard myosin light chain kinase, therefore, requires other regions of the light chain in addition to a phosphate acceptor site.",

author = "Lukas, {Thomas J.} and Anne Redelfs and Burgess, {Wilson H.} and Watterson, {D. Martin}",

note = "Funding Information: {\textquoteright} Supported in part by funds from National Institutes of Health Grant GM30953. {\textquoteleft}To whom correspondence should be addressed. 3 On leave of absence from School of Medicine, Tulane University, New Orleans, La. 4 Current Address: Department of Cell Biology, Revlon Biotechnology Research Center, Rockville, Md. {\textquoteright} Abbreviations used: PTH, phenylthiohydantoin; MLCK, myosin light chain kinase, Mops, 4-morpho-linepropanesulfonie acid; BSA, bovine serum albumin; TFA, trifluoroacetic acid; TPCK, L-l-ptosylamino-2-phenylethylchloromethyl ketone.",

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doi = "10.1016/0003-9861(85)90212-7",

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AU - Lukas, Thomas J.

AU - Redelfs, Anne

AU - Burgess, Wilson H.

AU - Watterson, D. Martin

N1 - Funding Information: ’ Supported in part by funds from National Institutes of Health Grant GM30953. ‘To whom correspondence should be addressed. 3 On leave of absence from School of Medicine, Tulane University, New Orleans, La. 4 Current Address: Department of Cell Biology, Revlon Biotechnology Research Center, Rockville, Md. ’ Abbreviations used: PTH, phenylthiohydantoin; MLCK, myosin light chain kinase, Mops, 4-morpho-linepropanesulfonie acid; BSA, bovine serum albumin; TFA, trifluoroacetic acid; TPCK, L-l-ptosylamino-2-phenylethylchloromethyl ketone.

PY - 1985/5/1

Y1 - 1985/5/1

N2 - Amino acid sequences of peptides containing the phosphorylation site of bovine cardiac myosin light chain (L2) were determined. The site was localized to a serine residue in the tentative amino terminus of the light chain and is homologous to phosphorylation sites in other myosin light chains. Phosphorylation of bovine cardiac light chain by chicken gizzard myosin light chain kinase was Ca2+-calmodulin dependent. Kinetic data gave a Km of 107; μm and a Vmax of 23.6 μmol min-1 mg-1. In contrast to what has been observed with smooth muscle light chains, neither the phosphorylation site fragment of the cardiac light chain nor a synthetic tetradecapeptide containing the phosphorylation site were effectively phosphorylated by the chicken gizzard kinase. Phosphorylation of cardiac myosin light chains by chicken gizzard myosin light chain kinase, therefore, requires other regions of the light chain in addition to a phosphate acceptor site.

AB - Amino acid sequences of peptides containing the phosphorylation site of bovine cardiac myosin light chain (L2) were determined. The site was localized to a serine residue in the tentative amino terminus of the light chain and is homologous to phosphorylation sites in other myosin light chains. Phosphorylation of bovine cardiac light chain by chicken gizzard myosin light chain kinase was Ca2+-calmodulin dependent. Kinetic data gave a Km of 107; μm and a Vmax of 23.6 μmol min-1 mg-1. In contrast to what has been observed with smooth muscle light chains, neither the phosphorylation site fragment of the cardiac light chain nor a synthetic tetradecapeptide containing the phosphorylation site were effectively phosphorylated by the chicken gizzard kinase. Phosphorylation of cardiac myosin light chains by chicken gizzard myosin light chain kinase, therefore, requires other regions of the light chain in addition to a phosphate acceptor site.

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Amino acid sequence of the phosphorylation site of bovine cardiac myosin light chain

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