ArticleJournal of bacteriology1996
Phenotypes of Bacillus subtilis mutants lacking multiple class A high-molecular-weight penicillin-binding proteins.
Article in Journal of bacteriology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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Who cites it
53 citing papers in PubMed, 97 citations in OpenAlex.
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- A Small Molecule Inhibitor of CTP Synthetase Identified by Differential Activity on aFrontiers in microbiology · 2020Article
- Bacillus subtilis cell diameter is determined by the opposing actions of two distinct cell wall synthetic systems.Nature microbiology · 2019Article
- The cell cycle regulator GpsB functions as cytosolic adaptor for multiple cell wall enzymes.Nature communications · 2019Article
- Functional redundancy of division specific penicillin-binding proteins in Bacillus subtilis.Molecular microbiology · 2017Article
- Identification of some main Streptococcus iniae associated proteins: relationship.Veterinary research communications · 2017Article
- YodL and YisK Possess Shape-Modifying Activities That Are Suppressed by Mutations in Bacillus subtilis mreB and mbl.Journal of bacteriology · 2016Article
- Discrete and overlapping functions of peptidoglycan synthases in growth, cell division and virulence of Listeria monocytogenes.Molecular microbiology · 2015Article
- Peptidoglycan transformations during Bacillus subtilis sporulation.Molecular microbiology · 2013Article
- Selective penicillin-binding protein imaging probes reveal substructure in bacterial cell division.ACS chemical biology · 2012Article
- Homologues of the Bacillus subtilis SpoVB protein are involved in cell wall metabolism.Journal of bacteriology · 2009Article
- Bacillus subtilis homologs of MviN (MurJ), the putative Escherichia coli lipid II flippase, are not essential for growth.Journal of bacteriology · 2009Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Examination of Bacillus subtilis strains containing multiple mutations affecting the class A high-molecular-weight penicillin-binding proteins (PBPs) 1, 2c, and 4 revealed a significant degree of redundancy in the functions of these three proteins. In rich media, loss of PBPs 2c and 4 resulted in no obvious phenotype. The slight growth and cell morphology defects associated with loss of PBP 1 were exacerbated by the additional loss of PBP 4 but not PBP 2c. Loss of all three of these PBPs slowed growth even further. In minimal medium, loss of PBPs 2c and 4 resulted in a slight growth defect. The decrease in growth rate caused by loss of PBP 1 was accentuated slightly by loss of PBP 2c and greatly by loss of PBP 4. Again, a lack of all three of these PBPs resulted in the slowest growth. Loss of PBP 1 resulted in a 22% reduction in the cell radius. Cultures of a strain lacking PBP 1 also contained some cells that were significantly longer than those produced by the wild type, and some of the rod-shaped cells appeared slightly bent. The additional loss of PBP 4 increased the number of longer cells in the culture. Slow growth caused by a mutation in prfA, a gene found in an operon with the gene encoding PBP 1, was unaffected by the additional loss of PBPs 2c and 4, whereas loss of both prfA and PBP 1 resulted in extremely slow growth and the production of highly bent cells.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.