Archaebacterial ATPases: Relationship to Other Ion-Translocating ATPase Families Examined in Terms of Immunological Cross-Reactivity1

Konishi, Jin; Denda, Kimitoshi; Oshima, Tairo; Wakagi, Takayoshi; Uchida, Etsuo; Ohsumi, Yoshinori; Anraku, Yasuhiro; Matsumoto, Takao; Wakabayashi, T.; Mukohata, Yasuo; Ihara, Kenji; Ken-ichi, Inatomi; Kato, Keitaro; Ohta, Toshiko; William, Sandborn; Yoshida, Masasuke

doi:10.1093/oxfordjournals.jbchem.a123241

Cited by 24 publications

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“…In addition, note that the pH i for M. sedula incubated at 25ЊC was similar to that for M. sedula incubated at 70ЊC. In studies of a similar organism, S. acidocaldarius, whose respiratory chain components have previously been examined (9,17,20,30,33), Lüben and Schäfer (21) found ⌬ values to be inside negative, in contrast to the positive inside values found for M. sedula in this study and those reported for other mesoacidophiles (Table 1). Thiobacillus ferrooxidans also was found to have an inside negative ⌬ when it was incubated at pH 3.0, in contrast to its optimum pH of about 2.0 (Table 1).…”

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confidence: 79%

Bioenergetic Response of the Extreme Thermoacidophile Metallosphaera sedula to Thermal and Nutritional Stresses

Peeples¹,

Kelly

1995

Appl Environ Microbiol

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The bioenergetic response of the extremely thermoacidophilic archaeon Metallosphaera sedula to thermal and nutritional stresses was examined. Continuous cultures (pH 2.0, 70؇C, and dilution rate of 0.05 h ؊1) in which the levels of Casamino Acids and ferrous iron in growth media were reduced by a step change of 25 to 50% resulted in higher levels of several proteins, including a 62-kDa protein immunologically related to the molecular chaperone designated thermophilic factor 55 in Sulfolobus shibatae (J. D. Trent, J. Osipiuk, and T. Pinkau, J. Bacteriol. 172:1478-1484, 1990), on sodium dodecyl sulfate-polyacrylamide gels. The 62-kDa protein was also noted at elevated levels in cells that had been shifted from 70 to either 80 or 85؇C. The proton motive force (⌬p), transmembrane pH (⌬pH), and membrane potential (⌬) were determined for samples obtained from continuous cultures (pH 2.0, 70؇C, and dilution rate of 0.05 h ؊1) and incubated under nutritionally and/or thermally stressed and unstressed conditions. At 70؇C under optimal growth conditions, M. sedula was typically found to have a ⌬p of approximately ؊190 to ؊200 mV, the result of an intracellular pH of 5.4 (extracellular pH, 2.0) and a ⌬ of ؉40 to ؉50 mV (positive inside). After cells had been shifted to either 80 or 85؇C, ⌬ decreased to nearly 0 mV and internal pH approached 4.0 within 4 h of the shift; respiratory activity, as evidenced by iron speciation in parallel temperature-shifted cultures on iron pyrite, had ceased by this point. If cultures shifted from 70 to 80؇C were shifted back to 70؇C after 4 h, cells were able to regain pyrite oxidation capacity and internal pH increased to nearly normal levels after 13 h. However, ⌬ remained close to 0 mV, possibly the result of enhanced ionic exchange with media upon thermal damage to cell membranes. Further, when M. sedula was subjected to an intermediate temperature shift from 73 to 79؇C, an increase in pyrite dissolution (ferric iron levels doubled) over that of the unshifted control at 73؇C was noted. The improvement in leaching was attributed to the synergistic effect of chemical and biological factors. As such, periodic exposure to higher temperatures, followed by a suitable recovery period, may provide a basis for improving bioleaching rates of acidophilic chemolithotrophs.

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confidence: 79%

Bioenergetic Response of the Extreme Thermoacidophile Metallosphaera sedula to Thermal and Nutritional Stresses

Peeples¹,

Kelly

1995

Appl Environ Microbiol

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“…Like the large subunit, when the Methanothrix 52-kDa subunit was compared with the 51and 52-kDa subunits of S. acidocaldarius (7) and H. halobium (14), respectively, 36 and 64% of the amino acid residues were found to be identical. Thus, the N-terminal amino acid sequences of the two large subunits of Methanothrix ATPase were homologous with those of other archaeal ATPases, suggesting that the Methanothrix ATPase also belongs to the V-type ATPase family (12,23).…”

Section: Resultsmentioning

confidence: 86%

Membrane ATPase from the aceticlastic methanogen Methanothrix thermophila

1993

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A new isolate of the aceticlastic methanogen Methanothrix thermophila utilizes only acetate as the sole carbon and energy source for methanogenesis (Y. Kamagata and E. Mikami, Int. J. Syst. Bacteriol. 41:191-196, 1991). ATPase activity in its membrane was found, and ATP hydrolysis activity in the pH range of 5.5 to 8.0 in the presence of Mg2+ was observed. It had maximum activity at around 70 degrees C and was specifically stimulated up to sixfold by 50 mM NaHSO3. The proton ATPase inhibitor N,N'-dicyclohexylcarbodiimide inhibited the membrane ATPase activity, but azide, a potent inhibitor of F0F1 ATPase (H(+)-translocating ATPase of oxidative phosphorylation), did not. Since the enzyme was tightly bound to the membranes and could not be solubilized with dilute buffer containing EDTA, the nonionic detergent nonanoyl-N-methylglucamide (0.5%) was used to solubilize it from the membranes. The purified ATPase complex in the presence of the detergent was also sensitive to N,N'-dicyclohexylcarbodiimide, and other properties were almost the same as those in the membrane-associated form. The purified enzyme revealed at least five kinds of subunits on a sodium dodecyl sulfate-polyacrylamide gel, and their molecular masses were estimated to be 67, 52, 37, 28, and 22 kDa, respectively. The N-terminal amino acid sequences of the 67- and 52-kDa subunits had much higher similarity with those of the 64 (alpha)- and 50 (beta)-kDa subunits of the Methanosarcina barkeri ATPase and were also similar to those of the corresponding subunits of other archaeal ATPases. The alpha beta complex of the M. barkeri ATPase has ATP-hydrolyzing activity, suggesting that a catalytic part of the Methanothrix ATPase contains at least the 67- and 52-kDa subunits.

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Transition from Protozoa to Metazoa: An Experimental Approach

Müller

1998

Molecular Evolution: Evidence for Monophyly of Metazoa

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Archaebacterial ATPases: Relationship to Other Ion-Translocating ATPase Families Examined in Terms of Immunological Cross-Reactivity1

Cited by 24 publications

References 0 publications

Bioenergetic Response of the Extreme Thermoacidophile Metallosphaera sedula to Thermal and Nutritional Stresses

Bioenergetic Response of the Extreme Thermoacidophile Metallosphaera sedula to Thermal and Nutritional Stresses

Membrane ATPase from the aceticlastic methanogen Methanothrix thermophila

Transition from Protozoa to Metazoa: An Experimental Approach

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