ArticleProceedings of the National Academy of Sciences of the United States of America2006
Different modes of SecY-SecA interactions revealed by site-directed in vivo photo-cross-linking.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.
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Who cites it
65 citing papers in PubMed, 119 citations in OpenAlex.
- Cryo-EM structure of the bacterial intramembrane metalloprotease RseP in the substrate-bound state.Science advances · 2025Article
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- Noncanonical Amino Acid Tools and Their Application to Membrane Protein Studies.Chemical reviews · 2024Review
- Cell surface protein-protein interaction profiling for biological network analysis and novel target discovery.Life medicine · 2024Review
- Noncanonical Amino Acids in Biocatalysis.Chemical reviews · 2024Review
- mRNA targeting eliminates the need for the signal recognition particle during membrane protein insertion in bacteria.Cell reports · 2023Article
- Repurposing Photosensitizer Proteins Through Genetic Code Expansion to Facilitate Photo-Biocatalysis.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Expanding the functionality of proteins with genetically encoded dibenzo[Chemical science · 2022Article
- The Dynamic SecYEG Translocon.Frontiers in molecular biosciences · 2021Review
- Article
- Biogenesis, quality control, and structural dynamics of proteins as explored in living cells via site-directed photocrosslinking.Protein science : a publication of the Protein Society · 2019Review
- Dynamic structural rearrangements and functional regulation of voltage-sensing phosphatase.The Journal of physiology · 2019Review
- Outer membrane lipoprotein RlpA is a novel periplasmic interaction partner of the cell division protein FtsK in Escherichia coli.Scientific reports · 2018Article
- The way is the goal: how SecA transports proteins across the cytoplasmic membrane in bacteria.FEMS microbiology letters · 2018Review
- Detailed Analyses of Stall Force Generation in Mycoplasma mobile Gliding.Biophysical journal · 2018Article
- A photo-cross-linking approach to monitor folding and assembly of newly synthesized proteins in a living cell.The Journal of biological chemistry · 2018Article
- The SecA protein deeply penetrates into the SecYEG channel during insertion, contacting most channel transmembrane helices and periplasmic regions.The Journal of biological chemistry · 2017Article
- Complementary Benzophenone Cross-Linking/Mass Spectrometry Photochemistry.Analytical chemistry · 2017Article
- Identification of Putative Substrates of SEC2, a Chloroplast Inner Envelope Translocase.Plant physiology · 2017Article
- YidC and SecYEG form a heterotetrameric protein translocation channel.Scientific reports · 2017Article
5 more citing papers are in PubMed but not listed here.
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
While the SecA ATPase drives protein translocation across the bacterial cytoplasmic membrane by interacting with the SecYEG translocon, molecular details of SecA-SecY interaction remain poorly understood. Here, we studied SecY-SecA interaction by using an in vivo site-directed cross-linking technique developed by Schultz and coworkers [Chin, J. W., Martin, A. B., King, D. S., Wang, L., Schultz, P. G. (2002) Proc. Natl. Acad. Sci. USA 99:11020-11024 and Chin, J. W., Schultz, P. G. (2002) ChemBioChem 3:1135-1137]. Benzoyl-phenylalanine introduced into specific SecY positions at the second, fourth, fifth, and sixth cytoplasmic domains allowed UV cross-linking with SecA. Cross-linked products exhibited two distinct electrophoretic mobilities. SecA cross-linking at the most C-terminal cytoplasmic region (C6) was specifically enhanced in the presence of NaN(3), which arrests the ATPase cycle, and this enhancement was canceled by cis placement of some secY mutations that affect SecY-SecA cooperation. In vitro experiments showed directly that SecA approaches C6 when it is engaging in ATP-dependent preprotein translocation. On the basis of these findings, we propose that the C6 tail of SecY interacts with the working form of SecA, whereas C4-C5 loops may offer constitutive SecA-binding sites.
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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.