Substrate recognition determinants of the mitogen-activated 70K S6 kinase from rat liver.
作者： H Flotow , G Thomas
DOI: 10.1016/S0021-9258(19)50696-2
关键词:
摘要: The mitogen-activated 70K S6 kinase has an apparent Km for 40 S ribosomal subunits of 0.25 microM. a synthetic peptide derived from the carboxyl terminus and containing all in vivo sites phosphorylation was 2.5-fold higher. A number shorter peptides revealed that substrate recognition determinants preferred site phosphorylation, Ser236, reside seven-amino acid stretch S6, residues 231-217. Critical to is block 3 consecutive arginines, especially Arg231 Arg233. In contrast, replacement Ser235 or with alanine little effect on Km. Based this data consensus sequence would be Arg-(Arg)-Arg-X-X-Ser-X. kinases known phosphorylate including cAMP-dependent protein C 92K II, were also tested their ability decapeptide critical determinants. Finally, putative autoinhibitory domain did not serve as enzyme but inhibit its activity, although much less effectively than
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