Conversion of active transport vesicles of Escherichia coli into oxidative phosphorylation vesicles

Mével-Ninio, Maryvonne; Yamamoto, Thomas

doi:10.1016/0005-2728(74)90112-1

Cited by 15 publications

(7 citation statements)

References 8 publications

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“…Everted (inside-out) vesicles bound only 15% as much G6P as did normally oriented vesicles. This percentage closely matches the efficiency of the eversion procedure (9). After a pretreatment of mild trypsin digestion, vesicles were markedly diminished in their ability to bind G6P.…”

supporting

confidence: 77%

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uhp-directed, glucose 6-phosphate membrane receptor in Escherichia coli

Goldenbaum¹,

Farmer²

1980

J Bacteriol

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Membrane vesicles were characterized for their ability to specifically bind ["4C]glucose 6-phosphate. Membranes prepared from a strain carrying a ColEl uhp hybrid plasmid showed significantly enhanced glucose 6-phosphate binding. It is hypothesized that glucose 6-phosphate binding to these membranes is due to a uhpR-directed, membrane-bound receptor which functions in regulation of the inducible uhpT gene product: the hexose phosphate permnease.Escherichia coli can actively transport exogenous hexose phosphates into the cell via an inducible permease (2). This permease is the product of the uhpT gene, and its synthesis is induced only by the presence of external glucose 6-phosphate (G6P) (12). Intracellular G6P or other hexose phosphates, such as fructose 6phosphate (F6P), found externally do not induce permease production (3). This regulatory phenomenon is termed exogenous induction, and others (13) have hypothesized the involvement of a membrane receptor which would specifically bind to exogenous G6P and then somehow allow uhpT gene activation. Kadner (7) has identified a regulatory element (uhpR) of the uhp genes. We present evidence that the uhpR gene product is a membrane-bound receptor, specific for external G6P.E. coli strain CSR603 (F-Strr Gal-Uhp+ Rec-) was provided by A. Sancar and has been described elsewhere (11). E. coli JA200 (F+ Str8 Gal' Uhp+) was provided by J. Carbon and described elsewhere (1). Four JA200 strains were provided, each carrying a hybrid ColEl plasmid known to contain the uhp genes (R. Essenberg, personal communication). These four JA200 strains are designated 17-47, 35-4, 40-33, and 14-9. Conjugation between each of the four JA200 donors and the CSR603 recipient was carried out (10), and conjugates receiving the CoIEl uhp plasmid were selected by screening on nutrient agar-yeast extract plates containing streptomycin (200 Atg/ml) and colicin El (10%, vol/vol).ColEl colicin was prepared from chloroformtreated cultures of E. coli strain DB 1187. This strain has been shown to be a highly efficient producer of colicin El and was provided by D. Berg, Washington University, St. Louis, Mo., whose procedure for colicin preparation was t Present address: Department of Biological Sciences, University of Texas, Austin, TX 78703. used. Selected conjugates were also tested to demonstrate their Gal-phenotype. The largest number of conjugates was found resulting from the cross with JA200-17-47, and one of these colonies was chosen for further study. This conjugate, containing the ColEl uhp plasmid, was designated CSR603-17-47.The conjugate strain was tested in our laboratory for the presence of multiple copies of the uhp genes. It was found (data not shown) that the induced rate of G6P uptake (initial velocity) was 5.5 times greater in the conjugate than in the same strain which did not contain the ColEl hybrid plasmid. Both strains displayed similar degrees of uhp inducibility, indicating the presence of normal regulation of the hexose phosphate transport process. These findings indicate that ...

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confidence: 77%

“…Also shown, vesicles made from CSR603 (lacking the plasmid) bound only 29% as much G6P as those from the strain harboring the plasmid. 'Vesicles were everted as described elsewhere (9). d Vesicles were pretreated at 370C for 10 min with 0.05% trypsin, then sedimented at 27,000 x g, and washed with phosphate buffer.…”

mentioning

confidence: 99%

uhp-directed, glucose 6-phosphate membrane receptor in Escherichia coli

Goldenbaum¹,

Farmer²

1980

J Bacteriol

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“…Disruption of whole cells, spheroplasts, or right-side-out vesicles ofE. coli by sonication or by exposure to shear forces (e.g., in a French pressure cell or Ribi cell fractionator) yields a population of relatively small closed vesicles (17,181,259,410); on the basis of evidence from freeze-cleave electron microscopy, these vesicles are predominantly in the inside-out configuration (17, 105). Biochemical examination indicated that they did not catalyze energy-dependent amino acid uptake at a significant rate (181,259), although they readily catalyzed respiration-driven proton uptake (171), oxidative phosphorylation (259), ATP hydrolysis (181), and ATP-dependent transhydrogenation (157,181); the latter two reactions were almost completely inhibited by antibodies to ATPase (157,181).…”

Section: Cytoplasmmentioning

confidence: 99%

Bacterial respiration.

Haddock¹,

Jones²

1977

Bacteriological Reviews

392

205

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“…Important information has come from the examination of mutants of Escherichia coli which lack this ATPase (for a review, see . Although the oxidation of substrates proceeds normally in ATPase-negative strains Schairer & Haddock, 1972;Simoni & Shallenberger, 1972;Nieuwenhuis, Kanner, Gutnick, Postma & Van Dam, 1973;Rosen, 1973;Cox, Gibson & McCann, 1974) respiration does not support the phosphorylation of ADP Gutnick, Kanner & Postma, 1972;Kobayashi, Kin & Anraku, 1974;Mevel-Ninio & Yamamoto, 1974). Thus, this ATPase is required for the synthesis of ATP during oxidative phosphorylation.…”

mentioning

confidence: 95%

ATP synthesis driven by a protonmotive force inStreptococcus lactis

Maloney

Wilson

1975

J. Membrain Biol.

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An electrochemical potential difference for hydrogen ions ( a protonmotive force) was artifically imposed across the membrane of the anaerobic bacterium Streptococcus lactis. When cells were exposed to the ionophore, valinomycin, the electrical gradient was established by a potassium diffusion potential. A chemical gradient of protons was established by manipulating the transmembrane pH gradient. When the protonmotive force attained a value of 215 mV or greater, net ATP synthesis was catalyzed by the membrane-bound Ca++, Mg++ -stimulated ATPase. This was true whether the protonmotive force was dominated by the membrane potential (negative inside) or the pH gradient (alkaline inside). Under these conditions, ATP synthesis could be blocked by the ATPase inhibitor, dicyclohexylcarbodiimide, or by ionophores which rendered the membrane specifically permeable to protons. These observations provide strong evidence in support of the chemiosmotic hypothesis, which states that the membrane-bound ATPase couples the inward movement of protons to the synthesis of ATP.

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Conversion of active transport vesicles of Escherichia coli into oxidative phosphorylation vesicles

Cited by 15 publications

References 8 publications

uhp-directed, glucose 6-phosphate membrane receptor in Escherichia coli

uhp-directed, glucose 6-phosphate membrane receptor in Escherichia coli

Bacterial respiration.

ATP synthesis driven by a protonmotive force inStreptococcus lactis

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