Skip to main content
PMC home page
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1981 Mar;78(3):1481–1484. doi: 10.1073/pnas.78.3.1481

Relationship between the Na+/H+ antiporter and Na+/substrate symport in Bacillus alcalophilus.

A A Guffanti, D E Cohn, H R Kaback, T A Krulwich
PMCID: PMC319154  PMID: 6262805

Abstract

The Na+/H+ antiporter of the obligate alkalophile Bacillus alcalophilus facilitates growth at alkaline pH and precludes growth below pH 8.5. Thus, nonalkalophilic mutant strains do not exhibit Na+/H+ antiport activity and, interestingly, such strains concomitantly lose the ability to catalyze Na+-dependent accumulation of alpha-aminoisobutyrate [Krulwich, T. A., Mandel, D. G. Bornstein, R. F. & Guffanti, A. A. (1979) Biochem. Biophys. Res. Commun. 91, 58-62]. Several other Na+-dependent transport systems are now documented in vesicles from the wild-type strain, and it is demonstrated that these systems are defective in vesicles from the nonalkalophilic mutant KM23. Surprisingly, the defect seems to result not from the loss of Na+/H+ antiport activity per se but from a pleiotropic defect in the Na+/substrate symporters themselves. Monensin, an ionophore that catalyzes Na+/H+ exchange, does not restore respiration-driven Na+/substrate symport in KM23 vesicles. Moreover, with KM23 vesicles, efflux of alpha-aminoisobutyrate, L-malate, and L-aspartate down their respective concentration gradients is not stimulated by Na+, in contrast to the observations with wild-type vesicles. Because monensin should ameliorate a simple defect in Na+/H+ antiport activity and the antiporter should not be required for Na+/substrate symport down a concentration gradient, the results suggest that there may be a direct relationship between the antiporter and various Na+/substrate symporters. One possibility is that the systems share a Na+-translocating subunit.

Full text

PDF
1484

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Brey R. N., Beck J. C., Rosen B. P. Cation/proton antiport systems in Escherichia coli. Biochem Biophys Res Commun. 1978 Aug 29;83(4):1588–1594. doi: 10.1016/0006-291x(78)91403-1. [DOI] [PubMed] [Google Scholar]
  2. Cohn D. E., Kaback H. R. Mechanism of the melibiose porter in membrane vesicles of Escherichia coli. Biochemistry. 1980 Sep 2;19(18):4237–4243. doi: 10.1021/bi00559a015. [DOI] [PubMed] [Google Scholar]
  3. Dills S. S., Apperson A., Schmidt M. R., Saier M. H., Jr Carbohydrate transport in bacteria. Microbiol Rev. 1980 Sep;44(3):385–418. doi: 10.1128/mr.44.3.385-418.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Guffanti A. A., Susman P., Blanco R., Krulwich T. A. The protonmotive force and alpha-aminoisobutyric acid transport in an obligately alkalophilic bacterium. J Biol Chem. 1978 Feb 10;253(3):708–715. [PubMed] [Google Scholar]
  5. Hong J. S. An ecf mutation in Escherichia coli pleiotropically affecting energy coupling in active transport but not generation or maintenance of membrane potential. J Biol Chem. 1977 Dec 10;252(23):8582–8588. [PubMed] [Google Scholar]
  6. Kaczorowski G. J., Kaback H. R. Mechanism of lactose translocation in membrane vesicles from Escherichia coli. 1. Effect of pH on efflux, exchange, and counterflow. Biochemistry. 1979 Aug 21;18(17):3691–3697. doi: 10.1021/bi00584a009. [DOI] [PubMed] [Google Scholar]
  7. Kaczorowski G. J., Robertson D. E., Kaback H. R. Mechanism of lactose translocation in membrane vesicles from Escherichia coli. 2. Effect of imposed delata psi, delta pH, and Delta mu H+. Biochemistry. 1979 Aug 21;18(17):3697–3704. doi: 10.1021/bi00584a010. [DOI] [PubMed] [Google Scholar]
  8. Kitada M., Horikoshi K. Sodium ion-stimulated alpha-[1-14C]aminoisobutyric acid uptake in alkalophilic Bacillus species. J Bacteriol. 1977 Sep;131(3):784–788. doi: 10.1128/jb.131.3.784-788.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Koyama N., Kiyomiya A., Nosoh Y. Na+-dependent uptake of amino acids by an alkalophilic Bacillus. FEBS Lett. 1976 Dec 15;72(1):77–78. doi: 10.1016/0014-5793(76)80816-2. [DOI] [PubMed] [Google Scholar]
  10. Krulwich T. A., Mandel K. G., Bornstein R. F., Guffanti A. A. A non-alkalophilic mutant of Bacillus alcalophilus lacks the Na+/H+ antiporter. Biochem Biophys Res Commun. 1979 Nov 14;91(1):58–62. doi: 10.1016/0006-291x(79)90582-5. [DOI] [PubMed] [Google Scholar]
  11. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  12. Lanyi J. K., Renthal R., MacDonald R. E. Light-induced glutamate transport in Halobacterium halobium envelope vesicles. II. Evidence that the driving force is a light-dependent sodium gradient. Biochemistry. 1976 Apr 20;15(8):1603–1610. doi: 10.1021/bi00653a002. [DOI] [PubMed] [Google Scholar]
  13. Lanyi J. K., Silverman M. P. Gating effects in Halobacterium halobium membrane transport. J Biol Chem. 1979 Jun 10;254(11):4750–4755. [PubMed] [Google Scholar]
  14. Lanyi J. K. The role of Na+ in transport processes of bacterial membranes. Biochim Biophys Acta. 1979 Dec 20;559(4):377–397. doi: 10.1016/0304-4157(79)90011-x. [DOI] [PubMed] [Google Scholar]
  15. Lewis R. J., Belkina S., Krulwich T. A. Alkalophiles have much higher cytochrome contents than conventional bacteria and than their own non-alkalophilic mutant derivatives. Biochem Biophys Res Commun. 1980 Jul 31;95(2):857–863. doi: 10.1016/0006-291x(80)90866-9. [DOI] [PubMed] [Google Scholar]
  16. Lopilato J., Tsuchiya T., Wilson T. H. Role of Na+ and Li+ in thiomethylgalactoside transport by the melibiose transport system of Escherichia coli. J Bacteriol. 1978 Apr;134(1):147–156. doi: 10.1128/jb.134.1.147-156.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Mandel K. G., Guffanti A. A., Krulwich T. A. Monovalent cation/proton antiporters in membrane vesicles from Bacillus alcalophilus. J Biol Chem. 1980 Aug 10;255(15):7391–7396. [PubMed] [Google Scholar]
  18. Mitchell P. Performance and conservation of osmotic work by proton-coupled solute porter systems. J Bioenerg. 1973 Jan;4(1):63–91. doi: 10.1007/BF01516051. [DOI] [PubMed] [Google Scholar]
  19. Schuldiner S., Fishkes H. Sodium-proton antiport in isolated membrane vesicles of Escherichia coli. Biochemistry. 1978 Feb 21;17(4):706–711. doi: 10.1021/bi00597a023. [DOI] [PubMed] [Google Scholar]
  20. Stock J., Roseman S. A sodium-dependent sugar co-transport system in bacteria. Biochem Biophys Res Commun. 1971 Jul 2;44(1):132–138. doi: 10.1016/s0006-291x(71)80168-7. [DOI] [PubMed] [Google Scholar]
  21. Tokuda H., Kaback H. R. Sodium-dependent methyl 1-thio-beta-D-galactopyranoside transport in membrane vesicles isolated from Salmonella typhimurium. Biochemistry. 1977 May 17;16(10):2130–2136. doi: 10.1021/bi00629a013. [DOI] [PubMed] [Google Scholar]
  22. Tsuchiya T., Takeda K. Extrusion of sodium ions energized by respiration and glycolysis in Escherichia coli. J Biochem. 1979 Jul;86(1):225–230. [PubMed] [Google Scholar]
  23. West I. C., Mitchell P. Proton/sodium ion antiport in Escherichia coli. Biochem J. 1974 Oct;144(1):87–90. doi: 10.1042/bj1440087. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Zilberstein D., Padan E., Schuldiner S. A single locus in Escherichia coli governs growth in alkaline pH and on carbon sources whose transport is sodium dependent. FEBS Lett. 1980 Jul 28;116(2):177–180. doi: 10.1016/0014-5793(80)80637-5. [DOI] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES