ArticleJournal of bacteriology2008
Effects of SecE depletion on the inner and outer membrane proteomes of Escherichia coli.
Article in Journal of bacteriology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 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.
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.
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Who cites it
24 citing papers in PubMed, 55 citations in OpenAlex.
- Blue Native PAGE Analysis of Bacterial Secretion Complexes.Methods in molecular biology (Clifton, N.J.) · 2024Article
- mRNA targeting eliminates the need for the signal recognition particle during membrane protein insertion in bacteria.Cell reports · 2023Article
- Efficient biosynthesis of (R)-mandelic acid from styrene oxide by an adaptive evolutionary Gluconobacter oxydans STA.Biotechnology for biofuels and bioproducts · 2023Article
- Folding and Insertion of Transmembrane Helices at the ER.International journal of molecular sciences · 2021Review
- Cotranslational recruitment of ribosomes in protocells recreates a translocon-independent mechanism of proteorhodopsin biogenesis.iScience · 2021Article
- The Dynamic SecYEG Translocon.Frontiers in molecular biosciences · 2021Review
- Posttranslational insertion of small membrane proteins by the bacterial signal recognition particle.PLoS biology · 2020Article
- Article
- SecA inhibitors as potential antimicrobial agents: differential actions on SecA-only and SecA-SecYEG protein-conducting channels.FEMS microbiology letters · 2018Review
- The bacterial Sec system is required for the organization and function of the MreB cytoskeleton.PLoS genetics · 2017Article
- Article
- Membrane protein insertion and assembly by the bacterial holo-translocon SecYEG-SecDF-YajC-YidC.The Biochemical journal · 2016Article
- Lytic Action of the Truncated yncE Gene in Escherichia coli.Current microbiology · 2016Article
- Identification of putative substrates for the periplasmic chaperone YfgM in Escherichia coli using quantitative proteomics.Molecular & cellular proteomics : MCP · 2015Article
- Specificity of SecYEG for PhoA precursors and SecA homologs on SecA protein-conducting channels.Biochemical and biophysical research communications · 2013Article
- Optimizing heterologous protein production in the periplasm of E. coli by regulating gene expression levels.Microbial cell factories · 2013Article
- Article
- Promiscuous targeting of polytopic membrane proteins to SecYEG or YidC by the Escherichia coli signal recognition particle.Molecular biology of the cell · 2012Article
- SecA alone can promote protein translocation and ion channel activity: SecYEG increases efficiency and signal peptide specificity.The Journal of biological chemistry · 2011Article
- Membrane localization of small proteins in Escherichia coli.The Journal of biological chemistry · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Sec translocon is a protein-conducting channel that allows polypeptides to be transferred across or integrated into a membrane. Although protein translocation and insertion in Escherichia coli have been studied using only a small set of specific model substrates, it is generally assumed that most secretory proteins and inner membrane proteins use the Sec translocon. Therefore, we have studied the role of the Sec translocon using subproteome analysis of cells depleted of the essential translocon component SecE. The steady-state proteomes and the proteome dynamics were evaluated using one- and two-dimensional gel analysis, followed by mass spectrometry-based protein identification and extensive immunoblotting. The analysis showed that upon SecE depletion (i) secretory proteins aggregated in the cytoplasm and the cytoplasmic sigma(32) stress response was induced, (ii) the accumulation of outer membrane proteins was reduced, with the exception of OmpA, Pal, and FadL, and (iii) the accumulation of a surprisingly large number of inner membrane proteins appeared to be unaffected or increased. These proteins lacked large translocated domains and/or consisted of only one or two transmembrane segments. Our study suggests that several secretory and inner membrane proteins can use Sec translocon-independent pathways or have superior access to the remaining Sec translocons present in SecE-depleted cells.
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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.