ArticleThe Journal of cell biology2012
Co-operation between different targeting pathways during integration of a membrane protein.
Article in The Journal of cell biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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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.
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Who cites it
27 citing papers in PubMed, 48 citations in OpenAlex.
- Review
- Twin-arginine transport complex plays an essential role inMolecular biology of the cell · 2026Article
- Twin-arginine transport complex plays an essential role inbioRxiv : the preprint server for biology · 2025Article
- The twin-arginine translocation system is vital for cell adhesion and uptake of iron in the cystic fibrosis pathogenVirulence · 2024Article
- Article
- Characterization of a TatA/TatB binding site on the TatC component of theMicrobiology (Reading, England) · 2023Article
- Bacterial Signal Peptides- Navigating the Journey of Proteins.Frontiers in physiology · 2022Review
- The Dynamic SecYEG Translocon.Frontiers in molecular biosciences · 2021Review
- A membrane-depolarizing toxin substrate of theProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Targeting of proteins to the twin-arginine translocation pathway.Molecular microbiology · 2020Review
- Ferric Citrate Regulator FecR Is Translocated across the Bacterial Inner Membrane via a Unique Twin-Arginine Transport-Dependent Mechanism.Journal of bacteriology · 2020Article
- Noncompetitive binding of PpiD and YidC to the SecYEG translocon expands the global view on the SecYEG interactome inThe Journal of biological chemistry · 2019Article
- Protein Export into and across the Atypical Diderm Cell Envelope of Mycobacteria.Microbiology spectrum · 2019Review
- Evolution of mitochondrial TAT translocases illustrates the loss of bacterial protein transport machines in mitochondria.BMC biology · 2018Article
- Genome wide identification and experimental validation of Pseudomonas aeruginosa Tat substrates.Scientific reports · 2018Article
- The Cellular Mechanisms that Ensure an Efficient Secretion in Streptomyces.Antibiotics (Basel, Switzerland) · 2018Review
- Article
- Article
- A signal sequence suppressor mutant that stabilizes an assembled state of the twin arginine translocase.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- The type VII secretion system of Staphylococcus aureus secretes a nuclease toxin that targets competitor bacteria.Nature microbiology · 2016Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Membrane protein assembly is a fundamental process in all cells. The membrane-bound Rieske iron-sulfur protein is an essential component of the cytochrome bc(1) and cytochrome b(6)f complexes, and it is exported across the energy-coupling membranes of bacteria and plants in a folded conformation by the twin arginine protein transport pathway (Tat) transport pathway. Although the Rieske protein in most organisms is a monotopic membrane protein, in actinobacteria, it is a polytopic protein with three transmembrane domains. In this work, we show that the Rieske protein of Streptomyces coelicolor requires both the Sec and the Tat pathways for its assembly. Genetic and biochemical approaches revealed that the initial two transmembrane domains were integrated into the membrane in a Sec-dependent manner, whereas integration of the third transmembrane domain, and thus the correct orientation of the iron-sulfur domain, required the activity of the Tat translocase. This work reveals an unprecedented co-operation between the mechanistically distinct Sec and Tat systems in the assembly of a single integral membrane protein.
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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.