ArticleProceedings of the National Academy of Sciences of the United States of America2013
Glycolipozyme MPIase is essential for topology inversion of SecG during preprotein translocation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Review
- Key contributions of a glycolipid to membrane protein integration.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2024Review
- Preparation of Uniformly Oriented Inverted Inner (Cytoplasmic) Membrane Vesicles from Gram-Negative Bacterial Cells.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Phosphatidylglycerol Is the Lipid Donor for Synthesis of Phospholipid-Linked Enterobacterial Common Antigen.Journal of bacteriology · 2023Article
- Interaction between glycolipid MPIase and proteinaceous factors during protein integration into the cytoplasmic membrane ofFrontiers in molecular biosciences · 2022Review
- The Dynamic SecYEG Translocon.Frontiers in molecular biosciences · 2021Review
- Article
- The bacterial protein YidC accelerates MPIase-dependent integration of membrane proteins.The Journal of biological chemistry · 2019Article
- The lipid-dependent structure and function of LacY can be recapitulated and analyzed in phospholipid-containing detergent micelles.Scientific reports · 2019Article
- Lipid-Assisted Membrane Protein Folding and Topogenesis.The protein journal · 2019Review
- Increased expression of the bacterial glycolipid MPIase is required for efficient protein translocation across membranes in cold conditions.The Journal of biological chemistry · 2019Article
- CdsA is involved in biosynthesis of glycolipid MPIase essential for membrane protein integration in vivo.Scientific reports · 2019Article
- The Sec System: Protein Export inEcoSal Plus · 2017Review
- Escherichia coli SecG is required for residual export mediated by mutant signal sequences and for SecY-SecE complex stability.Journal of bacteriology · 2015Article
- Lipids and topological rules governing membrane protein assembly.Biochimica et biophysica acta · 2014Review
- Capturing the bacterial holo-complex.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
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Authors and funding
5 authors.
Funding
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Abstract
Presecretory proteins are translocated across biological membranes through protein-conducting channels such as Sec61 (eukaryotes) and SecYEG (bacteria). SecA, a translocation ATPase, pushes preproteins out with dynamic structural changes through SecYEG. SecG, a subunit of the SecYEG channel possessing two transmembrane stretches (TMs), undergoes topology inversion coupled with SecA-dependent translocation. Recently, we characterized membrane protein integrase (MPIase), a glycolipozyme involved in not only protein integration into membranes but also preprotein translocation. We report here that SecG inversion occurs only when MPIase associates with SecYEG. We also found that MPIase modulates the dimer orientation of SecYEG. Cysteine-scanning mutagenesis mapped SecG TM 2 to a relatively hydrophilic environment. The dimer formation of SecG, crosslinked at TM 2, was not observed on SecG inversion, indicating that SecYEG undergoes a dynamic structural change during preprotein translocation.
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