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Identification of the sites in myelin basic protein that are phosphorylated by meiosis‐activated protein kinase p44 mpk
Author(s) -
Sanghera Jasbinder S.,
Aebersold Ruedi,
Morrison Hamish D.,
Bures Edward J.,
Pelech Steven L.
Publication year - 1990
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(90)81090-b
Subject(s) - threonine , biochemistry , edman degradation , protein kinase a , phosphorylation , serine , myelin basic protein , biology , peptide , peptide sequence , chemistry , microbiology and biotechnology , myelin , central nervous system , neuroscience , gene
Myelin basic protein serves as a convenient substrate for detection of a 44 kDa protein‐serine/threonine kinase (p44 mpk ) that is activated near the time of germinal vesicle breakdown in maturing echinoderm and amphibian oocytes. In vitro phosphorylation by purified p44 mpk from sea star oocytes was primarily on threonine residues on a single tryptic peptide of bovine brain myelin basic protein. Amino acid composition analysis of the isolated posphopeptide revealed that it was rich in proline residues. Automated solid‐phase sequencing by Edman degradation identified the major site as Thr‐97 in the sequence NIVTPRTPPPSQGK, which corresponds to residues 91–104 in bovine brain myelin basic protein. Thr‐94 was also phosphorylated by p44 mpk to a very minor extent.