ArticleJournal of bacteriology2002
Effects of lipoprotein biogenesis mutations on flagellar assembly in Salmonella.
Article in Journal of bacteriology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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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
8 citing papers in PubMed, 11 citations in OpenAlex.
- Identification and analysis of the crucial holin domain and sites and the bactericidal activity of a holin-endolysin lysis cassette from phage PZL-Ah152 againstJournal of virology · 2026Article
- Transcriptional Responses of Escherichia coli to a Small-Molecule Inhibitor of LolCDE, an Essential Component of the Lipoprotein Transport Pathway.Journal of bacteriology · 2016Article
- Microbial amyloids induce interleukin 17A (IL-17A) and IL-22 responses via Toll-like receptor 2 activation in the intestinal mucosa.Infection and immunity · 2012Article
- Article
- Direct visualization of red fluorescent lipoproteins indicates conservation of the membrane sorting rules in the family Enterobacteriaceae.Journal of bacteriology · 2006Article
- Additive effect on intracellular growth by Legionella pneumophila Icm/Dot proteins containing a lipobox motif.Infection and immunity · 2005Article
- Murein lipoprotein is a critical outer membrane component involved in Salmonella enterica serovar typhimurium systemic infection.Infection and immunity · 2005Article
- The two murein lipoproteins of Salmonella enterica serovar Typhimurium contribute to the virulence of the organism.Infection and immunity · 2004Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Flagellar assembly requires the expression of a large number of flagellum-specific genes. However, mutations in a number of other genes in Salmonella and Escherichia coli have been shown to have pleiotropic effects that affect flagellar assembly. FlgH (the L-ring subunit of the flagellar basal body) is a lipoprotein whose modification is important for L-ring assembly. We therefore tested whether the lack of motility of Salmonella mutants defective in lipoprotein biogenesis is a result of inability to modify FlgH. Our results show that temperature-sensitive apolipoprotein N-acyltransferase [lnt(Ts)] mutants are nonflagellate at 42 degrees C. However, the flagellar assembly defect occurs at a much earlier step in the pathway than L-ring assembly. These mutants failed to assemble even an MS ring, presumably because of the observed decrease in transcription of fliF. In contrast, temperature-sensitive diacylglycerol transferase [lgt(Ts)] mutants were motile at 42 degrees C, provided the strains carried an lpp (Braun lipoprotein) mutation to permit growth. We have isolated second-site mutants from an lgt(Ts) lpp(+) strain that grow but are nonflagellate at 42 degrees C. Thus, lipoprotein biogenesis is a factor that is important for flagellar assembly.
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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.