Evidence map›Paper›PMID 21856851›Full record

ArticleJournal of bacteriology2011

Nonclassical protein secretion by Bacillus subtilis in the stationary phase is not due to cell lysis.

Chun-Kai Yang, Hosam E Ewis, XiaoZhou Zhang, Chung-Dar Lu, Hae-Jin Hu, Yi Pan, Ahmed T Abdelal, Phang C Tai

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
6.4field-weighted citation impact, top 3% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

54 citing papers in PubMed, 108 citations in OpenAlex.

  1. Article
  2. Article
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  9. Moonlighting inMicroorganisms · 2021
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  10. "Applied and environmental microbiology · 2021
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  11. Article
  12. Article
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  14. Article
  15. Review
  16. The Ser/Thr protein kinase PrkC imprints phenotypic memory inThe Journal of biological chemistry · 2019
    Article
  17. Article
  18. Review
  19. Review
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 1 institution in 1 country.

Chun-Kai YangDepartment of Biology, Georgia State University, Atlanta, Georgia 30303, USA.
Hosam E Ewis
XiaoZhou Zhang
Chung-Dar Lu
Hae-Jin Hu
Yi Pan
Ahmed T Abdelal
Phang C Tai
Georgia State University · US

Funding

PROTEIN TRANSLOCATION &EXPORT IN GRAM-NEGATIVE BACTERIAR01GM034766 · NIGMS · GEORGIA STATE UNIVERSITY · PI TAI, PHANG C. · 1985 to 2005
$2.5M
NIGMS NIH HHS GM 34766NIGMS NIH HHS R01 GM034766
6 · The paper itself

Abstract

The carboxylesterase Est55 has been cloned and expressed in Bacillus subtilis strains. Est55, which lacks a classical, cleavable N-terminal signal sequence, was found to be secreted during the stationary phase of growth such that there is more Est55 in the medium than inside the cells. Several cytoplasmic proteins were also secreted in large amounts during late stationary phase, indicating that secretion in B. subtilis is not unique to Est55. These proteins, which all have defined cytoplasmic functions, include GroEL, DnaK, enolase, pyruvate dehydrogenase subunits PdhB and PdhD, and SodA. The release of Est55 and those proteins into the growth medium is not due to gross cell lysis, a conclusion that is supported by several lines of evidence: constant cell density and secretion in the presence of chloramphenicol, constant viability count, the absence of EF-Tu and SecA in the culture medium, and the lack of effect of autolysin-deficient mutants. The shedding of these proteins by membrane vesicles into the medium is minimal. More importantly, we have identified a hydrophobic α-helical domain within enolase that contributes to its secretion. Thus, upon the genetic deletion or replacement of a potential membrane-embedding domain, the secretion of plasmid gene-encoded mutant enolase is totally blocked, while the wild-type chromosomal enolase is secreted normally in the same cultures during the stationary phase, indicating differential specificity. We conclude that the secretion of Est55 and several cytoplasmic proteins without signal peptides in B. subtilis is a general phenomenon and is not a consequence of cell lysis or membrane shedding; instead, their secretion is through a process(es) in which protein domain structure plays a contributing factor.

Indexed as

Bacterial Secretion SystemsBacteriolysisAmino Acid SequenceBacillus subtilisBacterial ProteinsBase SequenceCarboxylesteraseGeobacillus stearothermophilusMolecular Sequence DataProtein Sorting SignalsProtein Structure, TertiaryProtein TransportBacterial ProteinsBacterial Secretion SystemsCarboxylesteraseProtein Sorting Signals

Identifiers

PMID21856851
PMCPMC3187209
OpenAlexW2131543532

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.