Identification of the amidotransferase AsnB1 as being responsible for meso-diaminopimelic acid amidation in lactobacillus plantarum peptidoglycan

• Published in: Journal of Bacteriology 22 (193), 6323 - 6330. (2011)
• Main Authors: Bernard, Elvis, Rolain, Thomas, Courtin, Pascal, Hols, Pascal
• Format: Publication
• Language: English
• Published: 2011
• Subjects: amidotransferase; bacterial-peptidoglycan; bactérie; diaminopimelic acid; effet immunitaire; lactobacillus plantarum; microbiology; peptide synthases

The peptidoglycan (PG) of Lactobacillus plantarum contains amidated meso-diaminopimelic acid (mDAP). The functional role of this PG modification has never been characterized in any bacterial species, except for its impact on PG recognition by receptors of the innate immune system. In silico analysis of loci carrying PG biosynthesis genes in the L. plantarum genome revealed the colocalization of the murE gene, which encodes the ligase catalyzing the addition of mDAP to UDP-N-muramoyl-D-glutamate PG precursors, with asnB1, which encodes a putative asparagine synthase with an N-terminal amidotransferase domain. By gene disruption and complementation experiments, we showed that asnB1 is the amidotransferase involved in mDAP amidation. PG structural analysis revealed that mDAP amidation plays a key role in the control of the L,D-carboxypeptidase DacB activity. In addition, a mutant strain with a defect in mDAP amidation is strongly affected in growth and cell morphology, with filamentation and cell chaining, while a DacB-negative strain displays a phenotype very similar to that of a wild-type strain. These results suggest that mDAP amidation may play a critical role in the control of the septation process.