ArticleJournal of bacteriology2014
Inefficient translation renders the Enterococcus faecalis fabK enoyl-acyl carrier protein reductase phenotypically cryptic.
Article in Journal of bacteriology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 20 citations in OpenAlex.
- A Single-Nucleotide Substitution Generates a de Novo Promoter That Activates a Latent Metabolic Bypass in Escherichia coli.Molecular microbiology · 2026Article
- Diverse unsaturated fatty acids bypass loss of FabH-catalysed initiation of fatty acid synthesis inMicrobiology (Reading, England) · 2026Article
- Perfectly Coupled Transcriptional Regulation of Fatty Acid Synthesis in Enterocci, Streptocci, and Lactococci.Molecular microbiology · 2026Article
- Elucidating the functions of fabF1 and fabF2 in Pseudomonas aeruginosa: implications for fatty acid metabolism and pathogenicity.BMC microbiology · 2026Article
- Defining the Enterococcus faecalis Fatty Acid Kinase System of Exogeneous Fatty Acid Utilization.Molecular microbiology · 2025Article
- Two putativeMicrobiology (Reading, England) · 2025Article
- Article
- The low enoyl-acyl carrier protein reductase activity of FabI2 is responsible for the high unsaturated fatty acid composition in Sinorhizobium meliloti.BMC microbiology · 2024Article
- The Enteric Bacterium Enterococcus faecalis Elongates and Incorporates Exogenous Short and Medium Chain Fatty Acids Into Membrane Lipids.Molecular microbiology · 2024Article
- Article
- Synthesis and evaluation of phenylimidazole FabK inhibitors as new Anti-C. Difficile agents.Bioorganic & medicinal chemistry · 2023Article
- Unsaturated fatty acid synthesis in Enterococcus faecalis requires a specific enoyl-ACP reductase.Molecular microbiology · 2022Article
- FabT, a Bacterial Transcriptional Repressor That Limits Futile Fatty Acid Biosynthesis.Microbiology and molecular biology reviews : MMBR · 2022Review
- TheFrontiers in microbiology · 2022Article
- Temperature regulation of membrane composition in the Firmicute, Enterococcus faecalis, parallels that of Escherichia coli.Environmental microbiology · 2021Article
- Article
- The Fatty Acid Synthesis Protein Enoyl-ACP Reductase II (FabK) is a Target for Narrow-Spectrum Antibacterials for Clostridium difficile Infection.ACS infectious diseases · 2019Article
- Bacterial fatty acid metabolism in modern antibiotic discovery.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2017Review
- Apigenin Impacts the Growth of the Gut Microbiota and Alters the Gene Expression of Enterococcus.Molecules (Basel, Switzerland) · 2017Article
- Escherichia coli enoyl-acyl carrier protein reductase (FabI) supports efficient operation of a functional reversal of β-oxidation cycle.Applied and environmental microbiology · 2015Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Enoyl-acyl carrier protein (ACP) reductase catalyzes the last step of the bacterial fatty acid elongation cycle. Enterococcus faecalis is unusual in that it encodes two unrelated enoyl-ACP reductases, FabI and FabK. We recently reported that deletion of the gene encoding FabI results in an unsaturated fatty acid (UFA) auxotroph despite the presence of fabK, a gene encoding a second fully functional enoyl-ACP reductase. By process of elimination, our prior report argued that poor expression was the reason that fabK failed to functionally replace FabI. We now report that FabK is indeed poorly expressed and that the expression defect is at the level of translation rather than transcription. We isolated four spontaneous mutants that allowed growth of the E. faecalis ΔfabI strain on fatty acid-free medium. Each mutational lesion (single base substitution or deletion) extended the fabK ribosome binding site. Inactivation of fabK blocked growth, indicating that the mutations acted only on fabK rather than a downstream gene. The mutations activated fabK translation to levels that supported fatty acid synthesis and hence cell growth. Furthermore, site-directed and random mutagenesis experiments showed that point mutations that resulted in increased complementarity to the 3' end of the 16S rRNA increased FabK translation to levels sufficient to support growth, whereas mutations that decreased complementarity blocked fabK translation.
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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.