ArticleIntegrative biology : quantitative biosciences from nano to macro2013
Determination of the quaternary structure of a bacterial ATP-binding cassette (ABC) transporter in living cells.
Article in Integrative biology : quantitative biosciences from nano to macro, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 36 citations in OpenAlex.
- Implementation of FRET Spectrometry Using Temporally Resolved Fluorescence: A Feasibility Study.International journal of molecular sciences · 2024Article
- Multiplexed imaging for probing RAS-RAF interactions in living cells.Biochimica et biophysica acta. Biomembranes · 2023Article
- Article
- The RTK Interactome: Overview and Perspective on RTK Heterointeractions.Chemical reviews · 2019Review
- Ab Initio Derivation of the FRET Equations Resolves Old Puzzles and Suggests Measurement Strategies.Biophysical journal · 2019Article
- New Techniques to Study Intracellular Receptors in Living Cells: Insights Into RIG-I-Like Receptor Signaling.Advances in experimental medicine and biology · 2019Review
- Site-Directed Fluorescence Approaches for Dynamic Structural Biology of Membrane Peptides and Proteins.Frontiers in molecular biosciences · 2019Review
- Fluorescence-based approaches for monitoring membrane receptor oligomerization.Journal of biosciences · 2018Review
- Quantitative microspectroscopic imaging reveals viral and cellular RNA helicase interactions in live cells.The Journal of biological chemistry · 2017Article
- FRET from single to multiplexed signaling events.Biophysical reviews · 2017Review
- Quaternary structures of opsin in live cells revealed by FRET spectrometry.The Biochemical journal · 2016Article
- The Transmembrane Domain of a Bicomponent ABC Transporter Exhibits Channel-Forming Activity.ACS chemical biology · 2016Article
- Fully quantified spectral imaging reveals in vivo membrane protein interactions.Integrative biology : quantitative biosciences from nano to macro · 2016Article
- Unliganded EphA3 dimerization promoted by the SAM domain.The Biochemical journal · 2015Article
- Experimental verification of the kinetic theory of FRET using optical microspectroscopy and obligate oligomers.Biophysical journal · 2015Article
- The sigma-1 receptors are present in monomeric and oligomeric forms in living cells in the presence and absence of ligands.The Biochemical journal · 2015Article
- The FRET signatures of noninteracting proteins in membranes: simulations and experiments.Biophysical journal · 2014Article
- Uninduced high-yield bacterial expression of fluorescent proteins.Analytical biochemistry · 2014Article
- Development and experimental testing of an optical micro-spectroscopic technique incorporating true line-scan excitation.International journal of molecular sciences · 2013Article
- FRET spectrometry: a new tool for the determination of protein quaternary structure in living cells.Biophysical journal · 2013Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Pseudomonas aeruginosa is a pathogenic Gram-negative bacterium that affects patients with cystic fibrosis and immunocompromised individuals. This bacterium coexpresses two unique forms of lipopolysaccharides (LPSs) on its surface, the A- and B-band LPS, which are among the main virulence factors that contribute to its pathogenicity. The polysaccharides in A-band LPSs are synthesized in the cytoplasm and translocated into the periplasm via an ATP-binding cassette (ABC) transporter consisting of a transmembrane protein, Wzm, and a cytoplasmic nucleotide-binding protein, Wzt. Most of the biochemical studies of A-band PSs in Pseudomonas aeruginosa are focused on the stages of the synthesis and ligation of PS, leaving the export stage involving the ABC transporter mostly unexplored. This difficulty is compounded by the fact that the subunit composition and structure of this bi-component ABC transporter are still unknown. Here we propose a simple but powerful method, based on Förster Resonance Energy Transfer (FRET) and optical micro-spectroscopy technology, to probe the structure of dynamic (as opposed to static) protein complexes in living cells. We use this method to determine the association stoichiometry and quaternary structure of the Wzm-Wzt complex in living cells. It is found that Wzt forms a rhombus-shaped homo-tetramer which becomes a square upon co-expression with Wzm, and that Wzm forms a square-shaped homo-tetramer both in the presence and absence of Wzt. Based on these results, we propose a structural model for the double-tetramer complex formed by the bi-component ABC transporter in living cells. An understanding of the structure and behavior of this ABC transporter will help develop antibiotics targeting the biosynthesis of the A-band LPS endotoxin.
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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.