Two-site phosphorylation of the phosphorylatable light chain (20-kDa light chain) of chicken gizzard myosin

When prepared under specified conditions chicken gizzard myosin was obtained which when incubated with ATP gave rise to a diphosphorylated as well as the monophosphorylated form of P light chain. Formation of the diphosphorylated light chain occurred more readily with these myosin preparations, but...

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Bibliographic Details
Published in:FEBS letters 1985-01, Vol.180 (2), p.165-169
Main Authors: Cole, H.A., Griffiths, H.S., Patchell, V.B., Perry, S.V.
Format: Article
Language:English
Subjects:
Adenosine Triphosphate - metabolism
Analytical, structural and metabolic biochemistry
Animals
Binding Sites
Biological and medical sciences
Chicken gizzard myosin
Chickens
Contractile proteins
Electrophoresis, Polyacrylamide Gel
Fundamental and applied biological sciences. Psychology
gizzard
Gizzard, Avian - enzymology
Holoproteins
muscles
myosin
Myosin light chain kinase
Myosins - metabolism
P light chain
Peptide Fragments - analysis
Phosphorylation
Protein Kinases - metabolism
Proteins
Two site phosphorylation
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Summary:When prepared under specified conditions chicken gizzard myosin was obtained which when incubated with ATP gave rise to a diphosphorylated as well as the monophosphorylated form of P light chain. Formation of the diphosphorylated light chain occurred more readily with these myosin preparations, but could also be obtained by prolonged incubation of the isolated whole light chain fraction with kinase preparations from rabbit skeletal and chicken gizzard muscles. Using isolated light chains as substrate the more readily formed monophosphorylated light chain contained serine phosphate while the diphosphorylated form contained serine and threonine phosphates.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(85)81064-4