Dynamics of cell wall-binding proteins at a single molecule level: B. subtilis autolysins show different kinds of motion.

ABSTRACT: The bacterial cell wall is a meshwork of crosslinked peptidoglycan strands, with a thickness of up to 50 nm in Firmicutes. Little is known about how proteins move through the cell wall to find sites of enzymatic activity. Cell wall synthesis for cell elongation involves the integration of new peptidoglycan strands by integral membrane proteins, as well as the degradation of existing strands by so-called autolysins, soluble proteins that are secreted through the cell membrane. Autolysins comprise different classes of proteases and glucanases and mostly contain cell-wall binding domains in addition to their catalytic domain. We have studied dynamics of Bacillus subtilis autolysins LytC, a major endopeptidase required for lateral cell wall growth, and LytF, a peptidase acting at the ne

SUBMITTER: Fiedler SM 

PROVIDER: S-EPMC11064672 | biostudies-literature | 2024 Apr

REPOSITORIES: biostudies-literature