Maltose transport system of <i>Escherichia coli</i>: An ABC‐type transporter

Nikaido, Hiroshi

doi:10.1016/0014-5793(94)00315-7

Cited by 82 publications

(64 citation statements)

References 27 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The stimulation is specific for HisJ because a number of HisJ mutant proteins were found that are unable to stimulate the ATPase activity. 7 HisQMP 2 also interacts with another soluble receptor, LAO (the periplasmic lysine-, arginine-, ornithine-binding protein) (28), which, therefore, would also be expected to stimulate the ATPase activity. Indeed, both unliganded and L-arginine-liganded LAO stimulate the activity.…”

Section: Permeabilization Of Pls Is Necessary Tomentioning

confidence: 99%

“…The superfamily includes bacterial periplasmic permeases, the yeast STE6 gene product, the mammalian P-glycoprotein (multidrug resistance protein or MDR), 1 the human cystic fibrosis transmembrane conductance regulator (CFTR), and the mammalian heterodimeric transporter (TAP1/TAP2) involved in antigen processing (3,4). The periplasmic histidine permease in Salmonella typhimurium and the maltose permease in Escherichia coli have been extensively characterized; both are good model systems for this superfamily (5)(6)(7).…”

mentioning

confidence: 99%

See 1 more Smart Citation

Characterization of the Adenosine Triphosphatase Activity of the Periplasmic Histidine Permease, a Traffic ATPase (ABC Transporter)

Liu

Ames

1997

Journal of Biological Chemistry

116

120

View full text Add to dashboard Cite

The superfamily of traffic ATPases (ABC transporters) includes bacterial periplasmic transport systems (permeases) and eukaryotic transporters. The histidine permease of Salmonella typhimurium is composed of a membrane-bound complex (HisQMP 2 ) containing four subunits, and of a soluble receptor, the histidine-binding protein (HisJ). Transport is energized by ATP. In this article the ATPase activity of HisQMP 2 has been characterized, using a novel assay that is independent of transport. The assay uses Mg 2؉ ions to permeabilize membrane vesicles or proteoliposomes, thus allowing access of ATP to both sides of the bilayer. HisQMP 2 displays a low level of intrinsic ATPase activity in the absence of HisJ; unliganded HisJ stimulates the activity and liganded HisJ stimulates to an even higher level. All three levels of activity display positive cooperativity for ATP with a Hill coefficient of 2 and a K 0.5 value of 0.6 mM. The activity has been characterized with respect to pH, salt, phospholipids, substrate, and inhibitor specificity. Free histidine has no effect.

show abstract

Section: Permeabilization Of Pls Is Necessary Tomentioning

confidence: 99%

mentioning

confidence: 99%

Characterization of the Adenosine Triphosphatase Activity of the Periplasmic Histidine Permease, a Traffic ATPase (ABC Transporter)

Liu

Ames

1997

Journal of Biological Chemistry

116

120

View full text Add to dashboard Cite

show abstract

“…This complex is composed of two hydrophobic proteins, MalF and MalG, and two copies of a cytoplasmic ATP-binding protein, MalK, forming the MalFGK2 complex (Davidson and Nikaido, 1990;. The system belongs to the superfamily of ATP-binding cassette (ABC) transporters (Nikaido, 1994), which share the same structural organization (for reviews, see Higgins, 1992;Doige and Ames, 1993). We report here that the overproduction of protein MalF in the absence of its membrane partners specifically induces the expression of the phtrA 24 -dependent promoter.…”

Section: Introductionmentioning

confidence: 99%

Heat shock induction by a misassembled cytoplasmic membrane protein complex in Escherichia coli

Mourez

Skouloubris

Betton

et al. 1997

Molecular Microbiology

View full text Add to dashboard Cite

SummaryWe analysed the effects of the overproduction of parts or all of a multisubunit ATP-binding cassette (ABC) transporter, the MalFGK2 complex, involved in the uptake of maltose and maltodextrins in Escherichia coli. We found that production of the MalF protein alone was inducing the phtrA promoter, which is under the control of a recently discovered sigma factor, 24 , involved in the response to extracytoplasmic stresses. The production level, stability and localization of MalF were not altered when produced without its partners, suggesting that the protein was correctly inserted in the membrane. Our results indicate that a large periplasmic loop located between the third and fourth transmembrane segment of MalF, the L3 loop, is responsible for phtrA induction: (i) deleted MalF proteins with no L3 loop or with a L3 loop lacking 120 amino acids do not induce the phtrA promoter; (ii) the export to the periplasm of the L3 loop alone or fused to MalE induces the phtrA promoter. Moreover, the proteolytic sensitivity of MalF is different when it is produced alone and when MalF and MalG are produced together, suggesting a change in the conformation and/or accessibility of MalF. These results suggest that some inner membrane proteins can be sensed outside the cytoplasm by a quality control apparatus or by the export machinery. Moreover, the observation of the phtrA induction by MalF could be a useful new tool for studying the insertion and assembly of the MalFGK2 complex.

show abstract

“…Here we extend the powerful HX MS technology to the two-domain, 370-residue, maltose binding protein (MBP). MBP is synthesized in the Escherichia coli cytoplasm and transported to the periplasm where it serves as a soluble receptor for the high-affinity capture and import of maltose and maltodextrins (20). The protein folds in vivo after deletion of a signal sequence (21); we study here the mature protein with the signal sequence deleted.…”

mentioning

confidence: 99%

Folding of a large protein at high structural resolution

Walters

Mayne²,

Hinshaw³

et al. 2013

Proc. Natl. Acad. Sci. U.S.A.

102

View full text Add to dashboard Cite

Kinetic folding of the large two-domain maltose binding protein (MBP; 370 residues) was studied at high structural resolution by an advanced hydrogen-exchange pulse-labeling mass-spectrometry method (HX MS). Dilution into folding conditions initiates a fast molecular collapse into a polyglobular conformation (<20 ms), determined by various methods including small angle X-ray scattering. The compaction produces a structurally heterogeneous state with widespread low-level HX protection and spectroscopic signals that match the equilibrium melting posttransition-state baseline. In a much slower step (7-s time constant), all of the MBP molecules, although initially heterogeneously structured, form the same distinct helix plus sheet folding intermediate with the same time constant. The intermediate is composed of segments that are distant in the MBP sequence but adjacent in the native protein where they close the longest residue-to-residue contact. Segments that are most HX protected in the early molecular collapse do not contribute to the initial intermediate, whereas the segments that do participate are among the less protected. The 7-s intermediate persists through the rest of the folding process. It contains the sites of three previously reported destabilizing mutations that greatly slow folding. These results indicate that the intermediate is an obligatory step on the MBP folding pathway. MBP then folds to the native state on a longer time scale (∼100 s), suggestively in more than one step, the first of which forms structure adjacent to the 7-s intermediate. These results add a large protein to the list of proteins known to fold through distinct native-like intermediates in distinct pathways.SAXS | HDX | protein collapse | denatured state ensemble F ifty years after Anfinsen's seminal demonstration that an unfolded protein can refold spontaneously when placed under native conditions, major questions concerning the folding process remain unanswered (1, 2). What is the unfolded state like, its degree of compaction, the reality and character of residual structure before folding begins, and its possible role in guiding the folding process (3-7)? Analogous questions relate to folding intermediates and the folding pathway itself. Do proteins fold through many alternative independent pathways as earlier theoretical investigations have suggested (8-12), or do they fold through necessary intermediates in a distinct pathway (13), as a growing list of experimental observations indicate (14, 15)? To answer these questions, it will be necessary to define experimentally the intermediate forms that proteins move through on their way to the native state. The problem has been that these transient states are beyond the reach of the usual high-resolution crystallographic and NMR structural methods. Most experimental folding studies have therefore relied on low-resolution optical methods that can follow folding in real time but rarely provide the structural information necessary to resolve the basic mechanistic questions.Recent work...

show abstract

Maltose transport system of Escherichia coli: An ABC‐type transporter

Cited by 82 publications

References 27 publications

Characterization of the Adenosine Triphosphatase Activity of the Periplasmic Histidine Permease, a Traffic ATPase (ABC Transporter)

Characterization of the Adenosine Triphosphatase Activity of the Periplasmic Histidine Permease, a Traffic ATPase (ABC Transporter)

Heat shock induction by a misassembled cytoplasmic membrane protein complex in Escherichia coli

Folding of a large protein at high structural resolution

Contact Info

Product

Resources

About