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Updated: May 27, 2026

Identification of Mycobacterium Species by DNA Microarray Chip Method
Published on: June 24, 2025
ChiZ levels modulate cell division process in mycobacteria
Indumathi S Vadrevu1, Hava Lofton, Krishna Sarva
1Biomedical Research, The University of Texas Health Science Center, Tyler, TX, USA.
Abstract:
We have previously shown that expression of chiZ (Rv2719c), encoding a cell wall hydrolase, is upregulated in response to DNA damaging agents and exposure to cephalexin. Furthermore, increased levels of ChiZ lead to decreased viability, loss of membrane integrity and defects in FtsZ-GFP localization and cell division. We now show that ChiZ N'-terminal 110 amino acid region, containing the cell wall hydrolase activity, is sufficient to modulate FtsZ-GFP localization. Further, we found that FtsZ-GFP rings are stabilized in a chiZ deletion strain indicating that ChiZ activity regulates FtsZ assembly. Overexpression of ftsZ did not reverse the reduction in viability caused by overproduction of ChiZ indicating that ChiZ neither interacts with nor directly influences FtsZ assembly. Bacterial two-hybrid assays revealed that ChiZ interacts with FtsI and FtsQ, two other septasomal proteins, but not with FtsZ. Finally, we show that ChiZ is not required for virulence of Mycobacterium tuberculosis in murine macrophages and mice. Our data suggest that optimal levels and activity of the cell wall hydrolase ChiZ are required for regulated cell division in mycobacteria.
Insights
Optimal levels of the cell wall hydrolase ChiZ are essential for regulated cell division in mycobacteria. ChiZ activity influences FtsZ assembly by interacting with other septasomal proteins, not FtsZ itself.
Area of Science:
- Microbiology
- Molecular Biology
- Cell Biology
Background:
- Cell wall hydrolase ChiZ (Rv2719c) expression increases with DNA damage and cephalexin exposure.
- Elevated ChiZ levels impair bacterial viability, membrane integrity, and cell division.
- ChiZ's role in regulating cell division requires further elucidation.
Purpose of the Study:
- To investigate the specific region of ChiZ responsible for modulating cell division.
- To determine how ChiZ activity impacts the assembly and regulation of FtsZ.
- To identify potential protein interactors of ChiZ involved in the cell division process.
Main Methods:
- Site-directed mutagenesis to identify the active region of ChiZ.
- Analysis of FtsZ-GFP localization and ring stabilization in wild-type and chiZ deletion strains.
- Bacterial two-hybrid assays to detect protein-protein interactions.
Main Results:
- The N'-terminal 110 amino acids of ChiZ, containing hydrolase activity, are sufficient to alter FtsZ-GFP localization.
- ChiZ deletion stabilizes FtsZ-GFP rings, indicating ChiZ regulates FtsZ assembly.
- ChiZ interacts with FtsI and FtsQ, but not FtsZ; ChiZ overexpression effects are not rescued by FtsZ overexpression.
- ChiZ is not essential for Mycobacterium tuberculosis virulence in vivo.
Conclusions:
- ChiZ activity is crucial for the proper regulation of FtsZ assembly and bacterial cell division.
- ChiZ likely influences cell division through interactions with other septasomal proteins.
- ChiZ is not implicated in Mycobacterium tuberculosis virulence.
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