Acidophilic character of yeast PID261/BUD32, a putative ancestor of eukaryotic protein kinases.
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.
Department of Biological Chemistry, and CRIBI, University of Padua, and Venetian Institute for Molecular Medicine, Viale G. Colombo 3, 35121, Padva, Italy.
Sonia
S
Facchin
Stefania
S
Sarno
Oriano
O
Marin
Raffaele
R
Lopreiato
Geppo
G
Sartori
Lorenzo A
LA
Pinna
D024342:Amino Acids, Acidic / Q000737:chemistry; D000818:Animals; D001665:Binding Sites; D005075:Biological Evolution; D047390:Casein Kinase II; D005057:Eukaryotic Cells / Q000201:enzymology*; D007700:Kinetics; D009154:Mutation; D010455:Peptides / Q000737:chemistry / Q000378:metabolism; D010766:Phosphorylation; D011485:Protein Binding; D017346:Protein Serine-Threonine Kinases / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000201:enzymology* / Q000235:genetics; D029701:Saccharomyces cerevisiae Proteins; D013379:Substrate Specificity
D024342:Amino Acids, Acidic; D010455:Peptides; D029701:Saccharomyces cerevisiae Proteins; C108301:BUD32 protein, S cerevisiae; D047390:Casein Kinase II; D017346:Protein Serine-Threonine Kinases