A lytic transglycosylase connects bacterial focal adhesion complexes to the peptidoglycan cell wall.

Abstract

The Gram-negative bacterium <i>Myxococcus xanthus</i> glides on solid surfaces. Dynamic bacterial focal adhesion complexes (bFACs) convert proton motive force from the inner membrane into mechanical propulsion on the cell surface. It is unclear how the mechanical force transmits across the rigid peptidoglycan (PG) cell wall. Here, we show that AgmT<i>,</i> a highly abundant lytic PG transglycosylase homologous to <i>Escherichia coli</i> MltG, couples bFACs to PG. Coprecipitation assay and single-particle microscopy reveal that the gliding motors fail to connect to PG and thus are unable to assemble into bFACs in the absence of an active AgmT. Heterologous expression of <i>E. coli</i> MltG restores the connection between PG and bFACs and thus rescues gliding motility in the <i>M. xanthus</i> cells that lack AgmT. Our results indicate that bFACs anchor to AgmT-modified PG to transmit mechanical force across the PG cell wall.