Acidophilic character of yeast PID261/BUD32, a putative ancestor of eukaryotic protein kinases

被引：13

作者：

Facchin, S

Sarno, S

Marin, O

Lopreiato, R

Sartori, G

Pinna, LA

机构：

[1] Univ Padua, Dept Biol Chem, I-35121 Padua, Italy

[2] Univ Padua, CRIBI, I-35121 Padua, Italy

[3] Venetian Inst Mol Med, I-35121 Padua, Italy

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2002年 / 296卷 / 05期

关键词：

YGR262c; piD261; Bud32; protein kinase; protein phosphorylation; evolution; yeast; archaea; casein kinase; CK2 beta subunit;

D O I：

10.1016/S0006-291X(02)02090-9

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Yeast piD261/Bud32 and its homologues are present in eukaryotes and in archaea but not in bacteria and are believed to make up a primordial branch of the eukaryotic protein kinase superfamily. Here, we show that, at variance with the majority of Ser/Thr protein kinases which recognize phosphoacceptor sites specified by basic and/or proline residues, piD261 phosphorylates in vitro a number of acidic proteins and peptides, and it recognizes seryl residues specified by carboxylic side chains. These data suggest that recognition of acidic sites might have been a primordial trait of protein kinases, which was modified during evolution to cope with the increasing complexity of protein phosphorylation in eukaryotes. (C) 2002 Elsevier Science (USA). All rights reserved.

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收藏

页码：1366 / 1371

页数：6

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