YvcK, a protein required for cell wall integrity and optimal carbon source utilization, binds uridine diphosphate-sugars

Elodie Foulquier (1, 2) , Anne Galinier (1, 3, 2)

1 LCB - Laboratoire de chimie bactérienne
2 IMM - Institut de Microbiologie de la Méditerranée
3 AMU - Aix Marseille Université

In Bacillus subtilis, Listeria monocytogenes and in two Mycobacteria, it was previously shown that yvcK is a gene required for normal cell shape, for optimal carbon source utilization and for virulence of pathogenic bacteria. Here we report that the B. subtilis protein YvcK binds to Uridine diphosphate-sugars like Uridine diphosphate-Glucose (UDP-Glc) and Uridine diphosphate-N-acetylglucosamine (UDP-GlcNAc) in vitro. Using the crystal structure of Bacillus halodurans YvcK, we identified residues involved in this interaction. We tested the effect of point mutations affecting the ability of YvcK to bind UDP-sugars on B. subtilis physiology and on cell size. Indeed, it was shown that UDP-Glc serves as a metabolic signal to regulate B. subtilis cell size. Interestingly, we observed that, whereas a yvcK deletion results in the formation of unusually large cells, inactivation of YvcK UDP-sugar binding site does not affect cell length. However, these point mutations result in an increased sensitivity to bacitracin, an antibiotic which targets peptidoglycan synthesis. We thus propose that UDP-GlcNAc, a precursor of peptidoglycan, could be a good physiological ligand candidate of YvcK.

Domaines: Génétique; Biologie cellulaire; Biochimie, Biologie Moléculaire; Sciences de l'environnement

Elodie Foulquier, Anne Galinier. YvcK, a protein required for cell wall integrity and optimal carbon source utilization, binds uridine diphosphate-sugars. Scientific Reports, 2017, 7 (1), ⟨10.1038/s41598-017-04064-2⟩. ⟨hal-01640047⟩