ArticleJournal of bacteriology2012
Secretion genes as determinants of Bacillus anthracis chain length.
Article in Journal of bacteriology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
28 citing papers in PubMed, 42 citations in OpenAlex.
- Assembly, architecture and functional roles of microbial surface layers.Nature reviews. Microbiology · 2026Review
- Heme A Synthase Deficiency Affects the Ability ofInternational journal of molecular sciences · 2022Article
- Dynamic Profile of S-Layer Proteins Controls Surface Properties of EmeticFrontiers in microbiology · 2022Article
- Article
- S-layers: The Proteinaceous Multifunctional Armors of Gram-Positive Pathogens.Frontiers in microbiology · 2021Review
- TheMicroorganisms · 2020Review
- The Structure ofInternational journal of molecular sciences · 2020Article
- Protein Export into and across the Atypical Diderm Cell Envelope of Mycobacteria.Microbiology spectrum · 2019Review
- The Two Distinct Types of SecA2-Dependent Export Systems.Microbiology spectrum · 2019Review
- PatB1 is an O-acetyltransferase that decorates secondary cell wall polysaccharides.Nature chemical biology · 2018Article
- Assembly and Function of the Bacillus anthracis S-Layer.Annual review of microbiology · 2017Review
- The CodY-dependent clhAB2 operon is involved in cell shape, chaining and autolysis in Bacillus cereus ATCC 14579.PloS one · 2017Article
- Genes Required for Bacillus anthracis Secondary Cell Wall Polysaccharide Synthesis.Journal of bacteriology · 2017Article
- Not just an antibiotic target: Exploring the role of type I signal peptidase in bacterial virulence.Bioorganic & medicinal chemistry · 2016Article
- Plantazolicin is an ultra-narrow spectrum antibiotic that targets theACS infectious diseases · 2016Article
- Structural Similarities and Differences between Two Functionally Distinct SecA Proteins, Mycobacterium tuberculosis SecA1 and SecA2.Journal of bacteriology · 2015Article
- Bacillus anthracis lcp Genes Support Vegetative Growth, Envelope Assembly, and Spore Formation.Journal of bacteriology · 2015Article
- Bacillus anthracis tagO Is Required for Vegetative Growth and Secondary Cell Wall Polysaccharide Synthesis.Journal of bacteriology · 2015Article
- Bacillus anthracis SlaQ Promotes S-Layer Protein Assembly.Journal of bacteriology · 2015Article
- A prl mutation in SecY suppresses secretion and virulence defects of Listeria monocytogenes secA2 mutants.Journal of bacteriology · 2015Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Bacillus anthracis grows in chains of rod-shaped cells, a trait that contributes to its escape from phagocytic clearance in host tissues. Using a genetic approach to search for determinants of B. anthracis chain length, we identified mutants with insertional lesions in secA2. All isolated secA2 mutants exhibited an exaggerated chain length, whereas the dimensions of individual cells were not changed. Complementation studies revealed that slaP (S-layer assembly protein), a gene immediately downstream of secA2 on the B. anthracis chromosome, is also a determinant of chain length. Both secA2 and slaP are required for the efficient secretion of Sap and EA1 (Eag), the two S-layer proteins of B. anthracis, but not for the secretion of S-layer-associated proteins or of other secreted products. S-layer assembly via secA2 and slaP contributes to the proper positioning of BslO, the S-layer-associated protein, and murein hydrolase, which cleaves septal peptidoglycan to separate chains of bacilli. SlaP was found to be both soluble in the bacterial cytoplasm and associated with the membrane. The purification of soluble SlaP from B. anthracis-cleared lysates did not reveal a specific ligand, and the membrane association of SlaP was not dependent on SecA2, Sap, or EA1. We propose that SecA2 and SlaP promote the efficient secretion of S-layer proteins by modifying the general secretory pathway of B. anthracis to transport large amounts of Sap and EA1.
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Registered trials
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.