The Gonococcal NlpD Protein Facilitates Cell Separation by Activating Peptidoglycan Cleavage by AmiC

Journal of Bacteriology
Elizabeth A StohlH Steven Seifert

Abstract

Key steps in bacterial cell division are the synthesis and subsequent hydrolysis of septal peptidoglycan (PG), which allow efficient separation of daughter cells. Extensive studies in the Gram-negative, rod-shaped bacterium Escherichia coli have revealed that this hydrolysis is highly regulated spatially and temporally. Neisseria gonorrhoeae is an obligate Gram-negative, diplococcal pathogen and is the only causative agent of the sexually transmitted infection gonorrhea. We investigated how cell separation proceeds in this diplococcal organism. We demonstrated that deletion of the nlpD gene in strain FA1090 leads to poor growth and to an altered colony and cell morphology. An isopropyl-beta-d-galactopyranoside (IPTG)-regulated nlpD complemented construct can restore these defects only when IPTG is supplied in the growth medium. Thin-section transmission electron microscopy (TEM) revealed that the nlpD mutant strain grew in large clumps containing live and dead bacteria, which was consistent with deficient cell separation. Biochemical analyses of purified NlpD protein showed that it was able to bind purified PG. Finally, we showed that, although NlpD has no hydrolase activity itself, NlpD potentiates the hydrolytic activity of A...Continue Reading

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Citations

Jul 25, 2018·Antibiotics·Krizia M Pérez Medina, Joseph P Dillard
Mar 6, 2019·Molecular Biology and Evolution·Jenna GalliePaul B Rainey
Aug 24, 2017·Molecular Microbiology·Aleksandra ZielińskaMartin Thanbichler
Sep 8, 2021·Frontiers in Microbiology·Wanda M Figueroa-CuilanPamela J B Brown
Sep 10, 2021·The Journal of Infectious Diseases·Kathryn A MatthiasMargaret C Bash

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