Expression and characterization of penicillin-binding proteins in Burkholderia cenocepacia.
Putative penicillin-binding proteins (PBPs) were identified in the genome of the Burkholderia cenocepacia strain J2315 based on homology to E. coli PBPs. The three sequences identified as homologs of E. coli PBP1a, BCAL2021, BCAL0274, and BCAM2632, were cloned and expressed as His(6)-tagged fusion proteins in E. coli. The fusion proteins were isolated and shown to bind beta-lactams, indicating these putative PBPs have penicillin-binding activity.
Specht
Kimberly Musa
KM
Department of Chemistry and Biochemistry, Denison University, Granville, USA. spechtk@denison.edu
Sheetz
Kyle H
KH
Alexander
Courtney M
CM
Lamech
Lilian T
LT
O'Connor
Lauren H
LH
Walker
Dawn M
DM
Stevenson
Hilary P
HP
D001426:Bacterial Proteins / Q000235:genetics* / Q000378:metabolism*; D019117:Burkholderia / Q000201:enzymology*; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000235:genetics; D015870:Gene Expression; D006801:Humans; D046915:Penicillin-Binding Proteins / Q000235:genetics* / Q000378:metabolism*; D011485:Protein Binding; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D047090:beta-Lactams / Q000378:metabolism*
D001426:Bacterial Proteins; D046915:Penicillin-Binding Proteins; D011993:Recombinant Fusion Proteins; D047090:beta-Lactams