» Articles » PMID: 19854920

Nonfermentative Thermoalkaliphilic Growth is Restricted to Alkaline Environments

Overview
Date 2009 Oct 27
PMID 19854920
Citations 15
Authors
Affiliations
Soon will be listed here.
Abstract

Caldalkalibacillus thermarum strain TA2.A1 grew in pH-controlled batch culture containing a fermentable growth substrate (i.e., sucrose) from pH 7.5 to 10.0 with no significant change in the specific growth rate, suggesting that this bacterium was a facultative alkaliphile. However, when strain TA2.A1 was grown on a nonfermentable carbon source, such as succinate or malate, no growth was observed until the external pH was >9.0, suggesting that this bacterium was an obligate alkaliphile. Succinate transport and sucrose transport by strain TA2.A1 showed pH profiles similar to that of growth on these carbon sources, and the molar growth yield on sucrose was higher at pH 9.5 than at pH 7.5, despite the increased energy demands on the cell for intracellular pH regulation. Succinate transport, succinate-dependent oxygen consumption, and succinate dehydrogenase and F(1)F(o)-ATPase specific activities were all significantly lower in cultures of strain TA2.A1 grown at pH 7.5 than in those cultured at pH 9.5. No significant ATP synthesis via the F(1)F(o)-ATP synthase was detected until the external pH was >8.5. On the basis of these results, we propose that nonfermentative thermoalkaliphilic growth is specialized to function at high pH values, but not at pH values near neutral pH.

Citing Articles

Physiological relevance, localization and substrate specificity of the alternative (type II) mitochondrial NADH dehydrogenases of .

Juergens H, Mielgo-Gomez A, Godoy-Hernandez A, Ter Horst J, Nijenhuis J, McMillan D Front Microbiol. 2024; 15:1473869.

PMID: 39726963 PMC: 11670749. DOI: 10.3389/fmicb.2024.1473869.


Quantitative proteomics reveals oxygen-induced adaptations in TA2.A1 microaerobic chemostat cultures.

de Jong S, Wissink M, Yildirim K, Pabst M, van Loosdrecht M, McMillan D Front Microbiol. 2024; 15:1468929.

PMID: 39529675 PMC: 11551716. DOI: 10.3389/fmicb.2024.1468929.


Membrane proteome of the thermoalkaliphile TA2.A1.

de Jong S, Sorokin D, van Loosdrecht M, Pabst M, McMillan D Front Microbiol. 2023; 14:1228266.

PMID: 37577439 PMC: 10416648. DOI: 10.3389/fmicb.2023.1228266.


ATP binding by an FF ATP synthase ε subunit is pH dependent, suggesting a diversity of ε subunit functional regulation in bacteria.

Krah A, Vogelaar T, de Jong S, Claridge J, Bond P, McMillan D Front Mol Biosci. 2023; 10:1059673.

PMID: 36923639 PMC: 10010621. DOI: 10.3389/fmolb.2023.1059673.


Peripheral Membrane Proteins: Promising Therapeutic Targets across Domains of Life.

Boes D, Godoy-Hernandez A, McMillan D Membranes (Basel). 2021; 11(5).

PMID: 34066904 PMC: 8151925. DOI: 10.3390/membranes11050346.


References
1.
Markwell M, Haas S, Bieber L, Tolbert N . A modification of the Lowry procedure to simplify protein determination in membrane and lipoprotein samples. Anal Biochem. 1978; 87(1):206-10. DOI: 10.1016/0003-2697(78)90586-9. View

2.
Hoffmann A, Dimroth P . The ATPase of Bacillus alcalophilus. Purification and properties of the enzyme. Eur J Biochem. 1990; 194(2):423-30. DOI: 10.1111/j.1432-1033.1990.tb15635.x. View

3.
Meier T, Morgner N, Matthies D, Pogoryelov D, Keis S, Cook G . A tridecameric c ring of the adenosine triphosphate (ATP) synthase from the thermoalkaliphilic Bacillus sp. strain TA2.A1 facilitates ATP synthesis at low electrochemical proton potential. Mol Microbiol. 2007; 65(5):1181-92. DOI: 10.1111/j.1365-2958.2007.05857.x. View

4.
McMillan D, Keis S, Dimroth P, Cook G . A specific adaptation in the a subunit of thermoalkaliphilic F1FO-ATP synthase enables ATP synthesis at high pH but not at neutral pH values. J Biol Chem. 2007; 282(24):17395-404. DOI: 10.1074/jbc.M611709200. View

5.
Horikoshi K . Alkaliphiles: some applications of their products for biotechnology. Microbiol Mol Biol Rev. 1999; 63(4):735-50, table of contents. PMC: 98975. DOI: 10.1128/MMBR.63.4.735-750.1999. View