ArticleThe Journal of biological chemistry2008
Genetic toggling of alkaline phosphatase folding reveals signal peptides for all major modes of transport across the inner membrane of bacteria.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 52 citations in OpenAlex.
- Loss of the ESX-5 secretion locus inProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Optimized APEX2 peroxidase-mediated proximity labeling in fast- and slow-growing mycobacteria.Methods in enzymology · 2022Article
- An experiment-informed signal transduction model for the role of the Staphylococcus aureus MecR1 protein in β-lactam resistance.Scientific reports · 2019Article
- Article
- Periplasmic protein EipA determines envelope stress resistance and virulence in Brucella abortus.Molecular microbiology · 2019Article
- RD5-mediated lack of PE_PGRS and PPE-MPTR export in BCG vaccine strains results in strong reduction of antigenic repertoire but little impact on protection.PLoS pathogens · 2018Article
- Multiplexed Quantitation of Intraphagocyte Mycobacterium tuberculosis Secreted Protein Effectors.Cell reports · 2018Article
- Rhodococcus erythropolis as a host for expression, secretion and glycosylation of Mycobacterium tuberculosis proteins.Microbial cell factories · 2017Article
- Article
- The PhoP-dependent ncRNA Mcr7 modulates the TAT secretion system in Mycobacterium tuberculosis.PLoS pathogens · 2014Article
- Article
- Twin-arginine translocase mutations that suppress folding quality control and permit export of misfolded substrate proteins.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Twin-arginine-dependent translocation of folded proteins.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2012Review
- The ins and outs of Mycobacterium tuberculosis protein export.Tuberculosis (Edinburgh, Scotland) · 2012Review
- Tat-dependent translocation of an F420-binding protein of Mycobacterium tuberculosis.PloS one · 2012Article
- Transmembrane insertion of twin-arginine signal peptides is driven by TatC and regulated by TatB.Nature communications · 2012Article
- Early contacts between substrate proteins and TatA translocase component in twin-arginine translocation.The Journal of biological chemistry · 2011Article
- Chlamydia trachomatis secretion of an immunodominant hypothetical protein (CT795) into host cell cytoplasm.Journal of bacteriology · 2011Article
- TatB functions as an oligomeric binding site for folded Tat precursor proteins.Molecular biology of the cell · 2010Article
- Protein export systems of Mycobacterium tuberculosis: novel targets for drug development?Future microbiology · 2010Review
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Prediction of export pathway specificity in prokaryotes is a challenging endeavor due to the similar overall architecture of N-terminal signal peptides for the Sec-, SRP- (signal recognition particle), and Tat (twin arginine translocation)-dependent pathways. Thus, we sought to create a facile experimental strategy for unbiased discovery of pathway specificity conferred by N-terminal signals. Using a limited collection of Escherichia coli strains that allow protein oxidation in the cytoplasm or, conversely, disable protein oxidation in the periplasm, we were able to discriminate the specific mode of export for PhoA (alkaline phosphatase) fusions to signal peptides for all of the major modes of transport across the inner membrane (Sec, SRP, or Tat). Based on these findings, we developed a mini-Tn5 phoA approach to isolate pathway-specific export signals from libraries of random fusions between exported proteins and the phoA gene. Interestingly, we observed that reduced PhoA was exported in a Tat-independent manner when targeted for Tat export in the absence of the essential translocon component TatC. This suggests that initial docking to TatC serves as a key specificity determinant for Tat-specific routing of PhoA, and in its absence, substrates can be rerouted to the Sec pathway, provided they remain compatible with the Sec export mechanism. Finally, the utility of our approach was demonstrated by experimental verification that four secreted proteins from Mycobacterium tuberculosis carrying putative Tat signals are bona fide Tat substrates and thus represent potential Tat-dependent virulence factors in this important human pathogen.
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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.