ReviewThe protein journal2019
Structural Basis of the Sec Translocon and YidC Revealed Through X-ray Crystallography.
Review in The protein journal, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 21 citations in OpenAlex.
- Substrate-induced assembly and functional mechanism of the membrane protein insertase SecYEG-YidC.The EMBO journal · 2026Article
- Membrane insertion of mitochondrial-encoded proteins regulates ribosome decoding speed.Nature structural & molecular biology · 2026Article
- AFM observation of protein translocation mediated by one unit of SecYEG-SecA complex.Nature communications · 2025Article
- Article
- Patchy and widespread distribution of bacterial translation arrest peptides associated with the protein localization machinery.Nature communications · 2024Article
- Key contributions of a glycolipid to membrane protein integration.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2024Review
- Dynamic feedback regulation for efficient membrane protein production using a small RNA-based genetic circuit in Escherichia coli.Microbial cell factories · 2022Article
- An investigation of the YidC-mediated membrane insertion of Pf3 coat protein using molecular dynamics simulations.Frontiers in molecular biosciences · 2022Article
- Search for translation arrest peptides encoded upstream of genes for components of protein localization pathways.Nucleic acids research · 2021Article
- Crossing the Vacuolar Rubicon: Structural Insights into Effector Protein Trafficking in Apicomplexan Parasites.Microorganisms · 2020Review
- Cardiolipin is required in vivo for the stability of bacterial translocon and optimal membrane protein translocation and insertion.Scientific reports · 2020Article
- The big BAM theory: An open and closed case?Biochimica et biophysica acta. Biomembranes · 2020Review
- Highlighting membrane protein structure and function: A celebration of the Protein Data Bank.The Journal of biological chemistryReview
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein translocation and membrane integration are fundamental, conserved processes. After or during ribosomal protein synthesis, precursor proteins containing an N-terminal signal sequence are directed to a conserved membrane protein complex called the Sec translocon (also known as the Sec translocase) in the endoplasmic reticulum membrane in eukaryotic cells, or the cytoplasmic membrane in bacteria. The Sec translocon comprises the Sec61 complex in eukaryotic cells, or the SecY complex in bacteria, and mediates translocation of substrate proteins across/into the membrane. Several membrane proteins are associated with the Sec translocon. In Escherichia coli, the membrane protein YidC functions not only as a chaperone for membrane protein biogenesis along with the Sec translocon, but also as an independent membrane protein insertase. To understand the molecular mechanism underlying these dynamic processes at the membrane, high-resolution structural models of these proteins are needed. This review focuses on X-ray crystallographic analyses of the Sec translocon and YidC and discusses the structural basis for protein translocation and integration.
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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.