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Phosphorylation site sequence of smooth muscle myosin light chain ( M r = 20 000)
Author(s) -
Pearson R.B.,
Jakes R.,
John M.,
Kendrick-Jones J.,
Kemp B.E.
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)80216-1
Subject(s) - myosin , myosin light chain kinase , immunoglobulin light chain , chain (unit) , phosphorylation , sequence (biology) , chemistry , biophysics , biochemistry , biology , genetics , physics , astronomy , antibody
The amino terminal sequence of the myosin light chain ( M r = 20 000) isolated from chicken gizzards was found to be acetyl‐Ser‐Ser‐Lys‐Arg‐Ala‐Lys‐Ala‐Lys‐Thr‐Thr‐Lys‐Lys‐Arg‐Pro‐Gln‐Arg‐Ala‐Thr‐Ser(P)‐Asn‐Val‐Phe. This sequence assignment differs from that reported by Maita et al. [(1981) European J. Biochem. 117, 417] in the order of the tryptic peptides. The revised amino acid sequence exhibits greater homology with the phosphorylation site sequences of the regulatory light chains from cardiac and skeletal muscle. Moreover it is now apparent why synthetic peptides corresponding to the previously reported sequence were very poor substrates for the myosin light chain kinase.