ArticleThe Journal of biological chemistry2013
Lipid, detergent, and Coomassie Blue G-250 affect the migration of small membrane proteins in blue native gels: mitochondrial carriers migrate as monomers not dimers.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed, 65 citations in OpenAlex.
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- The peculiar properties of mitochondrial carriers of the SLC25 family.The Biochemical journal · 2025Review
- The Role of Mitochondrial Pyruvate Carrier in Neurological Disorders.Molecular neurobiology · 2025Review
- Membrane potential stimulates ADP import and ATP export by the mitochondrial ADP/ATP carrier due to its positively charged binding site.Science advances · 2024Article
- Human mitochondrial carriers of the SLC25 family function as monomers exchanging substrates with a ping-pong kinetic mechanism.The EMBO journal · 2024Article
- Trace gas oxidation sustains energy needs of a thermophilic archaeon at suboptimal temperatures.Nature communications · 2024Article
- Human mitochondrial ADP/ATP carrier SLC25A4 operates with a ping-pong kinetic mechanism.EMBO reports · 2023Article
- Fifty years of the mitochondrial pyruvate carrier: New insights into its structure, function, and inhibition.Acta physiologica (Oxford, England) · 2023Review
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- Uncoupling Proteins and Regulated Proton Leak in Mitochondria.International journal of molecular sciences · 2022Review
- A novel heteromeric pantothenate kinase complex in apicomplexan parasites.PLoS pathogens · 2021Article
- An Overview of Genomics, Phylogenomics and Proteomics Approaches in Ascomycota.Life (Basel, Switzerland) · 2020Review
- The SLC25 Carrier Family: Important Transport Proteins in Mitochondrial Physiology and Pathology.Physiology (Bethesda, Md.) · 2020Review
- The mitochondrial ADP/ATP carrier exists and functions as a monomer.Biochemical Society transactions · 2020Review
- Cardiolipin, conformation, and respiratory complex-dependent oligomerization of the major mitochondrial ADP/ATP carrier in yeast.Science advances · 2020Article
- On the Detection and Functional Significance of the Protein-Protein Interactions of Mitochondrial Transport Proteins.Biomolecules · 2020Review
- The mitochondrial carrier pathway transports non-canonical substrates with an odd number of transmembrane segments.BMC biology · 2020Article
- The yeast mitochondrial pyruvate carrier is a hetero-dimer in its functional state.The EMBO journal · 2019Article
- Kinetics of Membrane Protein-Detergent Interactions Depend on Protein Electrostatics.The journal of physical chemistry. B · 2018Article
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5 authors at 2 institutions in 1 country.
Funding
Abstract
Blue native gel electrophoresis is a popular method for the determination of the oligomeric state of membrane proteins. Studies using this technique have reported that mitochondrial carriers are dimeric (composed of two ∼32-kDa monomers) and, in some cases, can form physiologically relevant associations with other proteins. Here, we have scrutinized the behavior of the yeast mitochondrial ADP/ATP carrier AAC3 in blue native gels. We find that the apparent mass of AAC3 varies in a detergent- and lipid-dependent manner (from ∼60 to ∼130 kDa) that is not related to changes in the oligomeric state of the protein, but reflects differences in the associated detergent-lipid micelle and Coomassie Blue G-250 used in this technique. Higher oligomeric state species are only observed under less favorable solubilization conditions, consistent with aggregation of the protein. Calibration with an artificial covalent AAC3 dimer indicates that the mass observed for solubilized AAC3 and other mitochondrial carriers corresponds to a monomer. Size exclusion chromatography of purified AAC3 in dodecyl maltoside under blue native gel-like conditions shows that the mass of the monomer is ∼120 kDa, but appears smaller on gels (∼60 kDa) due to the unusually high amount of bound negatively charged dye, which increases the electrophoretic mobility of the protein-detergent-dye micelle complex. Our results show that bound lipid, detergent, and Coomassie stain alter the behavior of mitochondrial carriers on gels, which is likely to be true for other small membrane proteins where the associated lipid-detergent micelle is large when compared with the mass of the protein.
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