ArticleProtein science : a publication of the Protein Society2018
Penetration into membrane of amino-terminal region of SecA when associated with SecYEG in active complexes.
Article in Protein science : a publication of the Protein Society, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 26 citations in OpenAlex.
- A unifying mechanism for protein transport through the core bacterial Sec machinery.Open biology · 2023Review
- Atomic Force Microscopy Reveals Complexity Underlying General Secretory System Activity.International journal of molecular sciences · 2022Review
- Topology of the SecA ATPase Bound to Large Unilamellar Vesicles.Journal of molecular biology · 2022Article
- Towards a Quantitative Understanding of Protein-Lipid Bilayer Interactions at the Single Molecule Level: Opportunities and Challenges.The Journal of membrane biology · 2021Review
- The SecA ATPase motor protein binds to Escherichia coli liposomes only as monomers.Biochimica et biophysica acta. Biomembranes · 2020Article
- Interaction of the motor protein SecA and the bacterial protein translocation channel SecYEG in the absence of ATP.Nanoscale advances · 2020Article
- Binding of SecA ATPase monomers and dimers to lipid vesicles.Biochimica et biophysica acta. Biomembranes · 2020Article
- Molecular Mimicry of SecA and Signal Recognition Particle Binding to the Bacterial Ribosome.mBio · 2019Article
- SecA-Mediated Protein Translocation through the SecYEG Channel.Microbiology spectrum · 2019Review
- Structure of the substrate-engaged SecA-SecY protein translocation machine.Nature communications · 2019Article
- Direct visualization of theScience advances · 2019Article
- Substrate Proteins Take Shape at an Improved Bacterial Translocon.Journal of bacteriology · 2019Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
The general secretory (Sec) system of Escherichia coli translocates both periplasmic and outer membrane proteins through the cytoplasmic membrane. The pathway through the membrane is provided by a highly conserved translocon, which in E. coli comprises two heterotrimeric integral membrane complexes, SecY, SecE, and SecG (SecYEG), and SecD, SecF, and YajC (SecDF/YajC). SecA is an associated ATPase that is essential to the function of the Sec system. SecA plays two roles, it targets precursors to the translocon with the help of SecB and it provides energy via hydrolysis of ATP. SecA exists both free in the cytoplasm and integrally membrane associated. Here we describe details of association of the amino-terminal region of SecA with membrane. We use site-directed spin labelling and electron paramagnetic resonance spectroscopy to show that when SecA is co-assembled into lipids with SecYEG to yield highly active translocons, the N-terminal region of SecA penetrates the membrane and lies at the interface between the polar and the hydrophobic regions, parallel to the plane of the membrane at a depth of approximately 5 Å. When SecA is bound to SecYEG, preassembled into proteoliposomes, or nonspecifically bound to lipids in the absence of SecYEG, the N-terminal region penetrates more deeply (8 Å). Implications of partitioning of the SecA N-terminal region into lipids on the complex between SecB carrying a precursor and SecA are discussed.
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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.