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.
Facchin
Sonia
S
Department of Biological Chemistry, and CRIBI, University of Padua, and Venetian Institute for Molecular Medicine, Viale G. Colombo 3, 35121, Padva, Italy.
Sarno
Stefania
S
Marin
Oriano
O
Lopreiato
Raffaele
R
Sartori
Geppo
G
Pinna
Lorenzo A
LA
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