ArticleScientific reports2019
Characterization of putative DD-carboxypeptidase-encoding genes in Mycobacterium smegmatis.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 19 citations in OpenAlex.
- An activator of a two-component system controls cell separation and intrinsic drug resistance inProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Article
- An activator of a two-component system controls cell separation and intrinsic drug resistance inbioRxiv : the preprint server for biology · 2025Article
- The combinatorial deletion of mycobacterial dd-carboxypeptidases is readily tolerated in Mycobacterium smegmatis.Access microbiology · 2025Article
- Structural Insights into the Penicillin-Binding Protein 4 (DacB) fromInternational journal of molecular sciences · 2024Article
- LdtC Is a Key l,d-Transpeptidase for Peptidoglycan Assembly in Mycobacterium smegmatis.Journal of bacteriology · 2023Article
- Transposon mutagenesis ineLife · 2022Article
- Characterisation of a putative M23-domain containing protein in Mycobacterium tuberculosis.PloS one · 2021Article
- First Penicillin-Binding Protein Occupancy Patterns for 15 β-Lactams and β-Lactamase Inhibitors in Mycobacterium abscessus.Antimicrobial agents and chemotherapy · 2020Article
- Aureolic Acid Group of Agents as Potential Antituberculosis Drugs.Antibiotics (Basel, Switzerland) · 2020Article
- Microbial Musings - June 2020.Microbiology (Reading, England) · 2020Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Penicillin binding proteins (PBPs) are the target of numerous antimicrobial agents that disrupt bacterial cell wall synthesis. In mycobacteria, cell elongation occurs through insertion of nascent cell wall material in the sub-polar region, a process largely driven by High Molecular Weight PBPs. In contrast, the function of DD-carboxypeptidases (DD-CPases), which are Low Molecular Weight Class 1C PBPs, in mycobacteria remains poorly understood. Mycobacterium smegmatis encodes four putative DD-CPase homologues, which display homology to counterparts in Escherichia coli. Herein, we demonstrate that these are expressed in varying abundance during growth. Deletion of MSMEG_1661, MSMEG_2433 or MSMEG_2432, individually resulted in no defects in growth, cell morphology, drug susceptibility or spatial incorporation of new peptidoglycan. In contrast, deletion of MSMEG_6113 (dacB) was only possible in a merodiploid strain expressing the homologous M. tuberculosis operon encoding Rv3627c (dacB), Rv3626c, Rv3625c (mesJ) and Rv3624c (hpt), suggestive of essentiality. To investigate the role of this operon in mycobacterial growth, we depleted gene expression using anhydrotetracycline-responsive repressors and noted reduced bipolar peptidoglycan synthesis. These data point to a possible role for this four gene operon, which is highly conserved across all mycobacterial species, in regulating spatial localization of peptidoglycan synthesis.
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