» Articles » PMID: 9841664

Inorganic Cation Transport and Energy Transduction in Enterococcus Hirae and Other Streptococci

Overview
Specialty Microbiology
Date 1998 Dec 5
PMID 9841664
Citations 30
Authors
Affiliations
Soon will be listed here.
Abstract

Energy metabolism by bacteria is well understood from the chemiosmotic viewpoint. We know that bacteria extrude protons across the plasma membrane, establishing an electrochemical potential that provides the driving force for various kinds of physiological work. Among these are the uptake of sugars, amino acids, and other nutrients with the aid of secondary porters and the regulation of the cytoplasmic pH and of the cytoplasmic concentration of potassium and other ions. Bacteria live in diverse habitats and are often exposed to severe conditions. In some circumstances, a proton circulation cannot satisfy their requirements and must be supplemented with a complement of primary transport systems. This review is concerned with cation transport in the fermentative streptococci, particularly Enterococcus hirae. Streptococci lack respiratory chains, relying on glycolysis or arginine fermentation for the production of ATP. One of the major findings with E. hirae and other streptococci is that ATP plays a much more important role in transmembrane transport than it does in nonfermentative organisms, probably due to the inability of this organism to generate a large proton potential. The movements of cations in streptococci illustrate the interplay between a variety of primary and secondary modes of transport.

Citing Articles

Modeling control and transduction of electrochemical gradients in acid-stressed bacteria.

Benyamin M, Perisin M, Hellman C, Schwalm 3rd N, Jahnke J, Sund C iScience. 2023; 26(7):107140.

PMID: 37404371 PMC: 10316662. DOI: 10.1016/j.isci.2023.107140.


Enterococcus faecalis OG1RF Evolution at Low pH Selects Fusidate-Sensitive Mutants in Elongation Factor G and at High pH Selects Defects in Phosphate Transport.

Fitzgerald B, Wadud A, Slimak Z, Slonczewski J Appl Environ Microbiol. 2023; 89(6):e0046623.

PMID: 37272807 PMC: 10304957. DOI: 10.1128/aem.00466-23.


Integration of text mining and biological network analysis: Identification of essential genes in sulfate-reducing bacteria.

Saxena P, Rauniyar S, Thakur P, Singh R, Bomgni A, Alaba M Front Microbiol. 2023; 14:1086021.

PMID: 37125195 PMC: 10133479. DOI: 10.3389/fmicb.2023.1086021.


Redundant potassium transporter systems guarantee the survival of under stress conditions.

Acciarri G, Gizzi F, Torres Manno M, Stulke J, Espariz M, Blancato V Front Microbiol. 2023; 14:1117684.

PMID: 36846772 PMC: 9945522. DOI: 10.3389/fmicb.2023.1117684.


Genome-resolved metagenome and metatranscriptome analyses of thermophilic composting reveal key bacterial players and their metabolic interactions.

Braga L, Pereira R, Martins L, Moura L, Sanchez F, Patane J BMC Genomics. 2021; 22(1):652.

PMID: 34507539 PMC: 8434746. DOI: 10.1186/s12864-021-07957-9.


References
1.
Kobayashi H . A proton-translocating ATPase regulates pH of the bacterial cytoplasm. J Biol Chem. 1985; 260(1):72-6. View

2.
Fenoll A, Munoz R, Garcia E, de la Campa A . Molecular basis of the optochin-sensitive phenotype of pneumococcus: characterization of the genes encoding the F0 complex of the Streptococcus pneumoniae and Streptococcus oralis H(+)-ATPases. Mol Microbiol. 1994; 12(4):587-98. DOI: 10.1111/j.1365-2958.1994.tb01045.x. View

3.
Bakker E, Mangerich W . Interconversion of components of the bacterial proton motive force by electrogenic potassium transport. J Bacteriol. 1981; 147(3):820-6. PMC: 216117. DOI: 10.1128/jb.147.3.820-826.1981. View

4.
Bakker E, Harold F . Energy coupling to potassium transport in Streptococcus faecalis. Interplay of ATP and the protonmotive force. J Biol Chem. 1980; 255(2):433-40. View

5.
Solioz M, Mathews S, Furst P . Cloning of the K+-ATPase of Streptococcus faecalis. Structural and evolutionary implications of its homology to the KdpB-protein of Escherichia coli. J Biol Chem. 1987; 262(15):7358-62. View