Characterization of the proteins encoded by the Bacillus subtilis yoxA-dacC operon.
In Bacillus subtilis, the yoxA and dacC genes were proposed to form an operon. The yoxA gene was overexpressed in Escherichia coli and its product fused to a polyhistidine tag was purified. An aldose-1-epimerase or mutarotase activity was measured with the YoxA protein that we propose to rename as GalM by analogy with its counterpart in E. coli. The peptide D-Glu-delta-m-A(2)pm-D-Ala-m-A(2)pm-D-Ala mimicking the B. subtilis and E. coli interpeptide bridge was synthesized and incubated with the purified dacC product, the PBP4a. A clear dd-endopeptidase activity was obtained with this penicillin-binding protein, or PBP. The possible role of this class of PBP, present in almost all bacteria, is discussed.
Duez
Colette
C
Centre d'Ingénierie des Protéines, Institut de Chimie B6a, Université de Liège, Liège, Belgium. cduez@ulg.ac.be
Zervosen
Astrid
A
Teller
Nathalie
N
Melkonian
Rémy
R
Banzubazé
Emmanuel
E
Bouillenne
Fabrice
F
Luxen
André
A
Frère
Jean-Marie
JM
D001412:Bacillus subtilis / Q000201:enzymology / Q000235:genetics*; D001426:Bacterial Proteins / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D010450:Endopeptidases / Q000235:genetics / Q000378:metabolism; D009876:Operon; D046915:Penicillin-Binding Proteins / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism
D001426:Bacterial Proteins; D046915:Penicillin-Binding Proteins; C019637:DD-endopeptidase; D010450:Endopeptidases