Abstract
Alkaliphiles grow under alkaline conditions that might be disadvantageous for the transmembrane pH gradient (ΔpH, outside acidic). In this study, the behaviors of extruded protons by the respiration of obligate alkaliphilic Bacillus clarkii K24-1U were investigated by comparison with those of neutralophilic Bacillus subtilis IAM 1026. Although whole-cell suspensions of both Bacillus species consumed oxygen immediately after the addition of air, there were lag times before the suspensions were acidified. Under alkaline conditions, the lag time for B. clarkii significantly increased, whereas that for B. subtilis decreased. In the presence of valinomycin or ETH-157, which disrupts the membrane electrical potential (Δψ), the cell suspensions of both Bacillus species acidified immediately after the addition of air. Artificial electroneutral antiporters (nigericin and monensin) that eliminate the ΔpH exhibited no significant effect on the lag times of the two Bacillus species except that monensin increased the lag times of B. clarkii. The inhibition of ATPase and the Na+ channel also exhibited little effects on the lag times. The increased lag time for B. clarkii may represent the Δψ-dependent proton retention on the outer surface of the cytoplasmic membrane to generate a sufficient ΔpH under alkaline conditions.
Similar content being viewed by others
References
Atsumi T, Maekawa Y, Tokuda H, Imae Y (1992) FEBS Lett 314:114–116
Avetisyan AV, Dibrov PA, Semeykina AL, Skulachev VP, Sokolov MV (1991) Biochim Biophys Acta 1098:95–104
Belevich I, Verkhovsky MI (2008) Antioxid Redox Signal 10:1–29
Blok MC, De Gier J, Van Deenen LL (1974) Biochim Biophys Acta 367:210–224
Branden G, Gennis RB, Brzezinski P (2006) Biochim Biophys Acta 1757:1052–1069
Cherepanov DA, Feniouk BA, Junge W, Mulkidjanian AY (2003) Biophys J 85:1307–1316
Fujinami S, Sato T, Trimmer JS, Spiller BW, Clapham DE, Krulwich TA, Kawagishi I, Ito M (2007) Microbiology 153:4027–4038
Graven SN, Estrada OS, Lardy HA (1966) Proc Natl Acad Sci USA 56:654–658
Guffanti AA, Mann M, Sherman TL, Krulwich TA (1984) J Bacteriol 159:448–452
Hase CC, Fedorova ND, Galperin MY, Dibrov PA (2001) Microbiol Mol Biol Rev 65:353–370
Hicks DB, Krulwich TA (1990) J Biol Chem 265:20547–20554
Hoffmann A, Dimroth P (1991) Eur J Biochem 196:493–497
Horikoshi K (1999) Microbiol Mol Biol Rev 63:735–750
Ito M, Xu H, Guffanti AA, Wei Y, Zvi L, Clapham DE, Krulwich TA (2004) Proc Natl Acad Sci USA 101:10566–10571
Jones CW, Brice JM, Downs AJ, Drozd JW (1975) Eur J Biochem 52:265–271
Kell DB, Hitchens GD (1982) Faraday Discuss Chem Soc 74:377–388
Kitada M, Horikoshi K (1992) J Bacteriol 174:5936–5940
Kleyman TR, Cragoe EJ Jr (1988) J Membr Biol 105:1–21
Krulwich TA (1986) J Membr Biol 89:113–125
Krulwich TA, Ito M, Gilmour R, Sturr MG, Guffanti AA, Hicks DB (1996) Biochim Biophys Acta 1275:21–26
Krulwich TA, Ito M, Gilmour R, Guffanti AA (1997) Extremophiles 1:163–169
Krulwich TA, Ito M, Gilmour R, Hicks DB, Guffanti AA (1998) Adv Microb Physiol 40:401–438
Krulwich TA, Ito M, Guffanti AA (2001) Biochim Biophys Acta 1505:158–168
Michel H, Oesterhelt D (1980) Biochemistry 19:4607–4614
Minohara S, Sakamoto J, Sone N (2002) J Biosci Bioeng 93:464–469
Mitchell P (1961) Nature 191:144–148
Mulkidjanian AY (2006) Biochim Biophys Acta 1757:415–427
Mulkidjanian AY, Heberle J, Cherepanov DA (2006) Biochim Biophys Acta 1757:913–930
Ogami S, Hijikata S, Tsukahara T, Mie Y, Matsuno T, Morita N, Hara I, Yamazaki K, Inoue N, Yokota A, Hoshino T, Yoshimune K, Yumoto I (2009) Extremophiles 13:491–504
Padan E, Bibi E, Ito M, Krulwich TA (2005) Biochim Biophys Acta 1717:67–88
Peddie CJ, Cook GM, Morgan HW (2000) Extremophiles 4:291–296
Pressman BC (1976) Annu Rev Biochem 45:501–530
Simon W, Carafoli E (1979) Methods Enzymol 56:439–448
Sone N, Fujiwara Y (1991) J Biochem 110:1016–1021
Sone N, Tsukita S, Sakamoto J (1999) J Biosci Bioeng 87:495–499
Sturr MG, Guffanti AA, Krulwich TA (1994) J Bacteriol 176:3111–3116
Sugiyama S, Cragoe EJ Jr, Imae Y (1988) J Biol Chem 263:8215–8219
Terahara N, Krulwich TA, Ito M (2008) Proc Natl Acad Sci USA 105:14359–14364
Vigne P, Frelin C, Cragoe EJ Jr, Lazdunski M (1983) Biochem Biophys Res Commun 116:86–90
Vigne P, Frelin C, Cragoe EJ Jr, Lazdunski M (1984) Mol Pharmacol 25:131–136
Yaginuma A, Tsukita S, Sakamoto J, Sone N (1997) J Biochem 122:969–976
Yumoto I (2002) J Biosci Bioeng 93:342–353
Author information
Authors and Affiliations
Corresponding author
Rights and permissions
About this article
Cite this article
Yoshimune, K., Morimoto, H., Hirano, Y. et al. The obligate alkaliphile Bacillus clarkii K24-1U retains extruded protons at the beginning of respiration. J Bioenerg Biomembr 42, 111–116 (2010). https://doi.org/10.1007/s10863-010-9278-7
Received:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1007/s10863-010-9278-7