Identification of the L,D-transpeptidases responsible for attachment of the Braun lipoprotein to Escherichia coli peptidoglycan.
The L,D-transpeptidase Ldt(fm) catalyzes peptidoglycan cross-linking in beta-lactam-resistant mutant strains of Enterococcus faecium. Here, we show that in Escherichia coli Ldt(fm) homologues are responsible for the attachment of the Braun lipoprotein to murein, indicating that evolutionarily related domains have been tailored to use muropeptides or proteins as acyl acceptors in the L,D-transpeptidation reaction.
Magnet
Sophie
S
INSERM, U655-LRMA, Université Pierre et Marie Curie, Centre de Recherches Biomédicales des Cordeliers, Paris, France. sophie.magnet@bhdc.jussieu.fr
Bellais
Samuel
S
Dubost
Lionel
L
Fourgeaud
Martine
M
Mainardi
Jean-Luc
JL
Petit-Frère
Sébastien
S
Marie
Arul
A
Mengin-Lecreulx
Dominique
D
Arthur
Michel
M
Gutmann
Laurent
L
D000595:Amino Acid Sequence; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics*; D029968:Escherichia coli Proteins / Q000235:genetics / Q000378:metabolism; D008074:Lipoproteins / Q000378:metabolism; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry / Q000378:metabolism; D010457:Peptidoglycan / Q000378:metabolism; D010458:Peptidyl Transferases / Q000235:genetics / Q000378:metabolism*
D029968:Escherichia coli Proteins; D008074:Lipoproteins; D010455:Peptides; D010457:Peptidoglycan; D010458:Peptidyl Transferases