ArticleBiochemical and biophysical research communications2014
An internal hydrophobic helical domain of Bacillus subtilis enolase is essential but not sufficient as a non-cleavable signal for its secretion.
Article in Biochemical and biophysical research communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
14 citing papers in PubMed, 26 citations in OpenAlex.
- Extracellular Glycolytic Activities in Root EndophyticMicroorganisms · 2022Article
- DnaK Functions as a Moonlighting Protein on the Surface ofFrontiers in microbiology · 2022Article
- Moonlighting inMicroorganisms · 2021Review
- "Applied and environmental microbiology · 2021Article
- Structural and Functional Dynamics ofMicroorganisms · 2019Article
- The Ser/Thr protein kinase PrkC imprints phenotypic memory inThe Journal of biological chemistry · 2019Article
- Review
- Protein moonlighting: what is it, and why is it important?Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018Review
- Intracellular proteins moonlighting as bacterial adhesion factors.AIMS microbiology · 2018Review
- Designing novel construction for cell surface display of protein E on Escherichia coli using non-classical pathway based on Lpp-OmpA.AMB Express · 2017Article
- Non-classical Protein Excretion Is Boosted by PSMα-Induced Cell Leakage.Cell reports · 2017Article
- Multimer recognition and secretion by the non-classical secretion pathway in Bacillus subtilis.Scientific reports · 2017Article
- A novel strategy for protein production using non-classical secretion pathway in Bacillus subtilis.Microbial cell factories · 2016Article
- Excretion of cytoplasmic proteins in Staphylococcus is most likely not due to cell lysis.Current genetics · 2016Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Many cytoplasmic proteins without a cleavable signal peptide, including enolase, are secreted during the stationary phase in Bacillus subtilis but the molecular mechanism is not yet clear. We previously identified a highly conserved embedded membrane domain in an internal hydrophobic α-helix of enolase that plays an important role in its secretion. In this study, we examined the role of the helix in more detail for the secretion of enolase. Altering this helix by mutations showed that many mutated forms in this domain were not secreted, some of which were not stable as a soluble form in the cytoplasm. On the other hand, mutations on the flanking regions of the helix or the conserved basic residues showed no deleterious effect. Bacillus enolase with the proper hydrophobic helical domain was also exported extracellularly in Escherichia coli, indicating that the requirement of the helix for the secretion of enolase is conserved in these species. GFP fusions with enolase regions showed that the hydrophobic helix domain itself was not sufficient to serve as a functional secretion signal; a minimal length of N-terminus 140 amino acids was required to mediate the secretion of the fused reporter GFP. We conclude that the internal hydrophobic helix of enolase is essential but is not sufficient as a signal for secretion; the intact long N-terminus including the hydrophobic helix domain is required to serve as a non-cleavable signal for the secretion of Bacillus enolase.
Indexed as
Identifiers
What OpenQuestion holds
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.