Escherichia coli has robust regulatory mechanisms against elevated peptidoglycan cleavage by lytic transglycosylases.

ABSTRACT: Peptidoglycan (PG) is an essential and conserved exoskeletal component in all bacteria that protects cells from lysis. Gram-negative bacteria such as Escherichia coli encode multiple redundant lytic transglycosylases (LTs) that engage in PG cleavage, a potentially lethal activity requiring proper regulation to prevent autolysis. To elucidate the potential effects and cellular regulatory mechanisms of elevated LT activity, we individually cloned the periplasmic domains of two membrane-bound LTs, MltA and MltB, under the control of the arabinose-inducible system for overexpression in the periplasmic space in E. coli. Interestingly, upon induction, the culture undergoes an initial period of cell lysis followed by robust growth restoration. The LT-overexpressing E. coli exhibits altered morpho

SUBMITTER: Liang Y 

PROVIDER: S-EPMC10139938 | biostudies-literature | 2023 Apr

REPOSITORIES: biostudies-literature