Identification of the sites in myelin basic protein that are phosphorylated by meiosis‐activated protein kinase p44 mpk

FEBS Letters

Bures, Edward J.²  Pelech, Steven L.¹  Morrison, Hamish D.²  Sanghera, Jasbinder S.²  Aebersold, Ruedi³ 

[1] Departments of Medicine, The University of British Columbia, Vancouver, BC V6T 1W5, Canada;The Biomedical Research Centre The University of British Columbia, Vancouver, BC V6T 1W5, Canada;Departments of Biochemistry The University of British Columbia, Vancouver, BC V6T 1W5, Canada

关键词: Myelin basic protein kinase;    MAP-2 kinase;    Meiosis;    cdc-2 kinase;    protein kinase encoded by homologs of the S. pombe cell division control-2 gene;    MBP;    myelin basic protein;    p42 MAP;    mitogen-activated microtubule-associated protein-2 kinase;    p44 mpk;    meiosis-activated MBP kinase;    TFA;    trifluoroacetic acid;   

DOI  :  10.1016/0014-5793(90)81090-B

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown