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How Bacteria Consume Their Own Exoskeletons (Turnover and Recycling of Cell Wall Peptidoglycan)
TLDR
Nine enzymes, one permease, and one periplasmic binding protein in E. coli that appear to have as their sole function the recovery of degradation products from peptidoglycan, thereby making them available for the cell to resynthesize more peptid glucose or to use as an energy source, have been identified.
Daughter cell separation is controlled by cytokinetic ring‐activated cell wall hydrolysis
TLDR
The results suggest that cellular amidase activity is regulated spatially and temporally by coupling their activation to the assembly of the cytokinetic ring.
An ATP-binding cassette transporter-like complex governs cell-wall hydrolysis at the bacterial cytokinetic ring
TLDR
FtsEX is identified as a regulator of cell-wall hydrolysis at the division site and ATP-binding cassette transporters, and it is demonstrated that FtsEX directly recruits EnvC to the septum via an interaction between EnVC and a periplasmic loop of FtsX.
LytM-Domain Factors Are Required for Daughter Cell Separation and Rapid Ampicillin-Induced Lysis in Escherichia coli
TLDR
E. coli thus appears to rely on two distinct sets of putative PG hydrolases to promote proper cell division, and the phenotypes of mutants lacking LytM-domain factors bear a striking resemblance to those of mutants defective for the N-acetylmuramyl-l-alanine amidases.
SEDS proteins are a widespread family of bacterial cell wall polymerases
TLDR
It is reported that, in Bacillus subtilis, this complex is functional in the absence of all known peptidoglycan polymerases, and these enzymes are core cell wall synthases of the cell elongation and division machinery, and represent attractive targets for antibiotic development.
A highly coordinated cell wall degradation machine governs spore morphogenesis in Bacillus subtilis.
TLDR
These activities provide a mechanism for processive cell wall degradation, supporting a model in which circumferentially distributed degradation machines function as motors pulling the mother cell membranes around the forespore.
An Anhydro-N-Acetylmuramyl-l-Alanine Amidase with Broad Specificity Tethered to the Outer Membrane of Escherichia coli
TLDR
AmiD cleaved the bond between MurNAc and l-alanine in both muropeptides and murein sacculi and demonstrated that AmpD and AmiD are the only enzymes present in E. coli that are able to cleave the anhMurNAc-l-Ala bond.
The N-Acetyl-d-Glucosamine Kinase of Escherichia coli and Its Role in Murein Recycling
TLDR
P purified GlcNAc kinase (NagK) from Escherichia coli cell extracts and identified the gene by determining the N-terminal sequence of the purified kinase, suggesting the existence of an alternative pathway (presumably repressed by Glcnac-6-P) that reutilizes Glc NAc without the involvement of NagK.
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