Peptidoglycan structure analysis of Lactococcus lactis reveals the presence of an L,D-carboxypeptidase involved in peptidoglycan maturation.
Detailed structural analysis of Lactococcus lactis peptidoglycan was achieved by identification of its constituent muropeptides separated by reverse phase high-performance liquid chromatography. Modification of the classical elution buffer allowed direct and sensitive analysis of the purified muropeptides by matrix-assisted laser desorption ionization-time of flight mass spectrometry. The structures of 45 muropeptides were assigned for L. lactis strain MG1363. Analysis of the muropeptide composition of an MG1363 dacB mutant showed that the dacB-encoded protein has l,d-carboxypeptidase activity and is involved in peptidoglycan maturation.
Courtin
Pascal
P
INRA, Unité de Biochimie Bactérienne, Domaine de Vilvert, 78352 Jouy-en-Josas Cedex, France.
Miranda
Guy
G
Guillot
Alain
A
Wessner
Françoise
F
Mézange
Christine
C
Domakova
Elena
E
Kulakauskas
Saulius
S
Chapot-Chartier
Marie-Pierre
MP
D001483:Base Sequence; D002268:Carboxypeptidases / Q000378:metabolism*; D002851:Chromatography, High Pressure Liquid; D017931:DNA Primers; D005784:Gene Amplification; D013294:Lactococcus lactis / Q000201:enzymology*; D010455:Peptides / Q000737:chemistry / Q000302:isolation & purification; D010457:Peptidoglycan / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*
D017931:DNA Primers; D010455:Peptides; D010457:Peptidoglycan; D002268:Carboxypeptidases