ArticleJournal of bioenergetics and biomembranes2001
Purification and characterization of the membrane-bound complex of an ABC transporter, the histidine permease.
Article in Journal of bioenergetics and biomembranes, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 39 citations in OpenAlex.
- Structure and function of Salmonella inner membrane.Archives of microbiology · 2026Review
- Microbial membrane transport genes in maize rhizosphere under fertilization - a preliminary study.Scientific reports · 2026Article
- Evidence from Mutational Analysis for a Single Transmembrane Substrate Binding Site in the Histidine ATP-Binding Cassette Transporter of Salmonella enterica Serovar Typhimurium.Journal of bacteriology · 2019Article
- Competitive Repression of theFrontiers in microbiology · 2019Article
- ATP-dependent Conformational Changes Trigger Substrate Capture and Release by an ECF-type Biotin Transporter.The Journal of biological chemistry · 2015Article
- Structural basis for substrate specificity of an amino acid ABC transporter.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- In vitro reassembly of the ribose ATP-binding cassette transporter reveals a distinct set of transport complexes.The Journal of biological chemistry · 2015Article
- The second extracellular loop of pore-forming subunits of ATP-binding cassette transporters for basic amino acids plays a crucial role in interaction with the cognate solute binding protein(s).Journal of bacteriology · 2010Article
- Biosynthesis of Histidine.EcoSal Plus · 2009Article
- Side chain and backbone contributions of Phe508 to CFTR folding.Nature structural & molecular biology · 2005Article
- Parasite plastids: maintenance and functions.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2003Article
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Authors and funding
6 authors at 1 institution in 1 country.
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Abstract
The bacterial histidine permease, an ABC transporter, from Salmonella typhimurium is composed of a membrane-bound complex, HisQMP2, comprising two hydrophobic subunits (HisQ and HisM), two copies of an ATP-hydrolyzing subunit, HisP, and a soluble receptor, HisJ. We describe the purification and characterization of HisQMP2 using a 6-histidines extension at the carboxy terminus of HisP [HisQMP2(his6)]. The purification is rapid and effective, giving a seven-fold purification with a yield of 85 and 98% purity. Two procedures are described differing in the detergent used (decanoylsucrose and octylglucoside, respectively) and in the presence of phospholipid. HisQMP2(his6) has ATPase and transport activities upon reconstitution into proteoliposomes (PLS). HisQMP2(his6) has a low level ATPase activity (intrinsic activity), which is stimulated to a different extent by the receptor--liganded and unliganded. Its pH optimum is 7.8-8.0, it requires a cation for activity and it displays cooperativity for ATP. The effect of various ATP analogs was analyzed. Determination of the molecular size of HisQMP2(his6) indicates that it is a monomer. The permeability properties of two kinds of reconstituted PLS preparations are described.
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