cDNA encoding a 59 kDa homolog of ribosomal protein S6 kinase from rabbit liver

FEBS Letters

Harmann, Beate¹  Kilimann, Manfred W.¹ 

[1] Institut für Physiologische Chemie, Abteilung für Biochemie Supramolekularer Systeme, Ruhr-Universität Bochum, D-4630 Bochum 1, FRG

关键词: S6 kinase;    Protein phosphorylation;    Cell cycle;    Mitogen;    Insulin;    Growth factor;   

DOI  :  10.1016/0014-5793(90)81096-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

We have isolated cDNA molecules encoding a protein with the characteristic sequence elements that are conserved between the catalytic domains of protein kinases. This protein is apparently a serine/threonine kinase and is most closely related to the amino-terminal half of the ribosomal protein S6 kinase II first characterized in Xenopus eggs (42% overall identity and 56% identity in the predicted catalytic domain). However, it clearly differs from S6 kinase II in that it has only one, rather than two predicted catalytic domains and a deduced molecular mass of 59109 Da. We propose that is may be more related to, or identical with, the mitogen-inducible S6 kinase of molecular mass 65–70 kDa described in mammalian liver, mouse 3T3 cells and chicken embryos. Remarkable structural features of the cDNA-encoded polypeptide are a section rich in proline, serine and threonine residues that resemble the multiphosphorylation domains of glycogen synthase and phosphorylase kinase a subunit, and a characteristic tyrosine residue in the putative nucleotide-binding glycine cluster which, by analogy to cdc2 kinase, is a potential tyrosine phosphorylation site.

【 授权许可】

Unknown