Energetics of sodium-dependent α-aminoisobutyric acid transport in the moderate halophile Vibrio costicola

Hamaide, Francette; Sprott, G. Dennis; Kushner, D. J.

doi:10.1016/0005-2728(84)90219-6

Cited by 19 publications

(21 citation statements)

References 31 publications

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“…Even with this organism, inhibition of transport at pH 8.5 was reduced 80% by 50 ,uM (0.5 ,umol/mg) TCS. Our findings with V. costicola confirm those of Hamaide et al (8), who observed that 20 ,uM (40 nmollmg) TCS or CCCP at pH 8.8 inhibited AIB transport into this organism 99 and 98%o, respectively.…”

Section: Discussionsupporting

confidence: 92%

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Sensitivity of some marine bacteria, a moderate halophile, and Escherichia coli to uncouplers at alkaline pH

1988

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The inhibitory effects of uncouplers on amino acid transport into three marine bacteria, Vibrio alginolyticus 118, Vibrio parahaemolyticus 113, and Alteromonas haloplanktis 214, into a moderate halophile, Vibrio costicola NRC 37001, and into Escherichia coli K-12 were found to vary depending upon the uncoupler tested, its concentration, and the pH. Higher concentrations of all of the uncouplers were required to inhibit transport at pH 8.5 than at pH 7.0. The protonophore carbonyl cyanide m-chlorophenylhydrazone showed the greatest reduction in inhibitory capacity as the pH was increased, carbonyl cyanide p-trifluoromethoxyphenylhydrazone showed less reduction, and 3,3',4',5-tetrachlorosalicylanilide was almost as effective as an inhibitor of amino acid transport at pH 8.5 as at pH 7.0 for all of the organisms except A. haloplanktis 214. Differences between the protonophores in their relative activities at pHs 7.0 and 8.5 were attributed to differences in their pK values. 3,3',4',5-Tetrachlorosalicylanilide, carbonyl cyanide m-chlorophenylhydrazone, 2-heptyl-4-hydroxyquinoline-N-oxide, and NaCN all inhibited Na+ extrusion from Na+-loaded cells of V. alginolyticus 118 at pH 8.5. The results support the conclusion that Na+ extrusion from this organism at pH 8.5 occurs as a result of Na+/H+ antiport activity. Data are presented indicating the presence in V. alginolyticus 118 of an NADH oxidase which is stimulated by Na+ at pH 8.5.In 1981, Tokuda and Unemoto (32) showed that the membrane potential (At) of K+-depleted and Na+-loaded Vibrio alginolyticus 138-2 was completely collapsed by 10 ,uM (4 nmol/mg of cell dry weight [in all references to concentration in this paper, the term in parentheses refers to the number of nanomoles or micromoles of the compound tested per milligram of cell dry weight]) carbonyl cyanide m-chlorophenylhydrazone (CCCP) at pH 6.0 to pH 7.0 but was only partially and transiently collapsed by this uncoupler at the same concentration at pH 8.5. They also found that respiration-dependent Na+ extrusion from the cells which occurred in the presence of K+ as well as Na+-dependent uptake of a-aminoisobutyric acid (AIB) was inhibited by 10 ,uM (2.2 nmol/mg) CCCP completely at pH 6.5 but only slightly at pH 8.5. To explain these observations the authors proposed the existence of a primary electrogenic Na+ extrusion system (Na+ pump) in V. alginolyticus 138-2 which they later concluded functioned at the Na+-activated NADH:quinone-acceptor oxidoreductase segment of the respiratory chain (35). Further evidence for the existence of an Na+ pump was obtained when mutants of V. alginolyticus 138-2 were isolated which showed (i) increased sensitivity to CCCP during growth, (ii) an Na+ extrusion mechanism which was sensitive to 10 ,uM (2.9 nmol/mg) CCCP, and (iii) NADH oxidase activity, no portion of which was stimulated by Na+ (28).Tsuchiya and Shinoda (36) observed respiration-driven Na+ extrusion from Vibrio parahaemolyticus at pH 8.5which was insensitive to 20 puM (3 nmol/mg) CCCP. KenDror et al. (16,17) ...

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Section: Discussionsupporting

confidence: 92%

“…The washed cells were suspended in 0.4 M NaCl at a cell density equivalent to 50 mg of protein per ml and maintained on ice. A sample of this suspension was diluted with a sufficient quantity of 50 mM Tricine-NaOH (pH 8 (31). RESULTS Effects on transport.…”

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confidence: 99%

Sensitivity of some marine bacteria, a moderate halophile, and Escherichia coli to uncouplers at alkaline pH

1988

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“…haloplanktis (Niven & MacLeod, 1980) and in V. alginolyticus . The moderately halophilic V. costicola was also shown to require ApNa+ for AIB uptake (Hamaide et al, 1984). Thus, the Na+-coupled transport systems were generally considered to be common in the marine and moderately halophilic bacteria.…”

Section: Discussionmentioning

confidence: 99%

“…Marine bacteria (Niven & MacLeod, 1980; and extreme halophiles (MacDonald et al, 1977;Lanyi, 1979) are known to require a sodium-motive force (ApNa+) for the active uptake of amino acids. The moderate halophile Vibrio costicola requires a A p N a + for active uptake of aaminoisobutyric acid (AIB) (Hamaide et al, 1984). Therefore, halophilic bacteria that require Na+ for optimal growth are generally considered to utilize A p N a + as the driving force of amino acid uptake.…”

Section: Introductionmentioning

confidence: 99%

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Correlation between the respiration-driven Na+ pump and Na+-dependent amino acid transport in moderately halophilic bacteria

Unemoto

Akagawa

Hayashi

1993

Journal of General Microbiology

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The effect of Na+ on amino acid uptake by moderately halophilic bacteria was examined using a-aminoisobutyric acid (AIB) as a nonmetabolizable amino acid analogue. Of the eight moderate halophiles investigated, the six Gram-negative bacteria that have a respiration-driven Na+ pump specifically required Na+ for AIB uptake. On the other hand, the two Gram-positive bacteria that have no respiration-driven Na+ pump showed no requirement for Na+ for AIB uptake. Thus, the mode of energy coupling to amino acid transport was quite different between the Gram-negative and Gram-positive moderate halophiles tested : the former, but not the latter, utilized Na+ circulation for the active uptake of AIB.

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Cellular Metabolism and Physiology of Hhalophilic Microorganisms

2003

Cellular Origin, Life in Extreme Habitats and Astrobiology

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Energetics of sodium-dependent α-aminoisobutyric acid transport in the moderate halophile Vibrio costicola

Cited by 19 publications

References 31 publications

Sensitivity of some marine bacteria, a moderate halophile, and Escherichia coli to uncouplers at alkaline pH

Sensitivity of some marine bacteria, a moderate halophile, and Escherichia coli to uncouplers at alkaline pH

Correlation between the respiration-driven Na+ pump and Na+-dependent amino acid transport in moderately halophilic bacteria

Cellular Metabolism and Physiology of Hhalophilic Microorganisms

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