Evidence map›Paper›PMID 23791875›Full record

ArticleBiochemical and biophysical research communications2013

Specificity of SecYEG for PhoA precursors and SecA homologs on SecA protein-conducting channels.

Hao Zhang, Ying-Hsin Hsieh, Bor-Ruei Lin, Liyan Yu, Hsiuchin Yang, Chun Jiang, Sen-Fang Sui, Phang C Tai

Abstract read
In one paragraph

Article in Biochemical and biophysical research communications, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
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

3 citing papers in PubMed.

  1. Review
  2. Article
  3. Mechanisms of Rose Bengal inhibition on SecA ATPase and ion channel activities.Biochemical and biophysical research communications · 2014
    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.

Hao Zhang *Department of Biology and Center of Biotechnology and Drug Design, Georgia State University, Atlanta, GA 30303.
Ying-Hsin Hsieh *Department of Biology and Center of Biotechnology and Drug Design, Georgia State University, Atlanta, GA 30303.
Bor-Ruei LinDepartment of Biology and Center of Biotechnology and Drug Design, Georgia State University, Atlanta, GA 30303.
Liyan YuDepartment of Biology and Center of Biotechnology and Drug Design, Georgia State University, Atlanta, GA 30303.
Hsiuchin YangDepartment of Biology and Center of Biotechnology and Drug Design, Georgia State University, Atlanta, GA 30303.
Chun JiangDepartment of Biology and Center of Biotechnology and Drug Design, Georgia State University, Atlanta, GA 30303.
Sen-Fang SuiState Key Laboratory of Biomembrane and Membrane Biotechnology, Center for Structural Biology, School of Life Sciences, Tsinghua University, Beijing, China 100084.
Phang C TaiDepartment of Biology and Center of Biotechnology and Drug Design, Georgia State University, Atlanta, GA 30303.

Funding

PROTEIN TRANSLOCATION &EXPORT IN GRAM-NEGATIVE BACTERIAR01GM034766 · NIGMS · GEORGIA STATE UNIVERSITY · PI TAI, PHANG C. · 1985 to 2005
$2.5M
NIGMS NIH HHS GM34766NIGMS NIH HHS R01 GM034766
6 · The paper itself

Abstract

Previous studies showed that Escherichia coli membranes depleted of SecYEG are capable of translocating certain precursor proteins, but not other precursors such as pPhoA, indicating a differential requirement for SecYEG. In this study, we examined the role of SecYEG in pPhoA translocation using a purified reconstituted SecA-liposomes system. We found that translocation of pPhoA, in contrast to that of pOmpA, requires the presence of purified SecYEG. A differential specificity of the SecYEG was also revealed in its interaction with SecA: EcSecYEG did not enhance SecA-mediated pOmpA translocation by purified SecA either from Pseudomonas aeruginosa or Bacillus subtilis. Neither was SecYEG required for eliciting ion channel activity, which could be opened by unfolded pPhoA or unfolded PhoA. Addition of the SecYEG complex did restore the specificity of signal peptide recognition in the ion-channel activity. We concluded that SecYEG confers specificity in interacting with protein precursors and SecAs.

Indexed as

AnimalsEscherichia coliEscherichia coli ProteinsProtein TransportSEC Translocation ChannelsXenopusEscherichia coli ProteinsSEC Translocation ChannelsChannel activitypPhoA translocationProtein-conducting channelSecA-liposomesSecYEG complex

Identifiers

PMID23791875
PMCPMC3740335

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Registered trials

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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.