» Articles » PMID: 28687653

Identification of the ATPase Subunit of the Primary Maltose Transporter in the Hyperthermophilic Anaerobe Thermotoga Maritima

Overview
Date 2017 Jul 9
PMID 28687653
Citations 7
Authors
Affiliations
Soon will be listed here.
Abstract

is a hyperthermophilic anaerobic bacterium that produces molecular hydrogen (H) by fermentation. It catabolizes a broad range of carbohydrates through the action of diverse ABC transporters. However, in and related species, highly similar genes with ambiguous annotation obscure a precise understanding of genome function. In , three putative genes, all annotated as ATPase subunits, exhibited high identity to each other. To distinguish between these genes, disruption mutants were constructed by gene replacement, and the resulting mutant cell lines were characterized. Only a disruption of produced a defect in maltose catabolism. To verify that the mutant phenotype arose specifically from inactivation, the mutation was repaired by recombination, and maltose catabolism was restored. This study demonstrates the importance of a maltose ABC-type transporter and its relationship to sugar metabolism in The application and further development of a genetic system was used here to investigate gene paralogs in the hyperthermophile The occurrence of three ABC transporter ATPase subunits all annotated as was evaluated using a combination of genetic and bioinformatic approaches. The results clarify the role of only one gene in maltose catabolism in a nonmodel organism noted for fermentative hydrogen production.

Citing Articles

G-quadruplex structures in 16S rRNA regions correlate with thermal adaptation in prokaryotes.

Lyu B, Niu K, Anderson D, Feng Q, Song Q Nucleic Acids Res. 2025; 53(3).

PMID: 39883013 PMC: 11780868. DOI: 10.1093/nar/gkaf042.


Sugar transport in thermophiles: Bridging lignocellulose deconstruction and bioconversion.

Tjo H, Conway J J Ind Microbiol Biotechnol. 2024; 51.

PMID: 38866721 PMC: 11212667. DOI: 10.1093/jimb/kuae020.


Improvement of CO and Acetate Coupling into Lactic Acid by Genetic Manipulation of the Hyperthermophilic Bacterium .

Esercizio N, Lanzilli M, Vastano M, Xu Z, Landi S, Caso L Microorganisms. 2021; 9(8).

PMID: 34442767 PMC: 8399208. DOI: 10.3390/microorganisms9081688.


Construction and Validation of a Genome-Scale Metabolic Network of Thermotoga sp. Strain RQ7.

Gautam J, Xu Z Appl Biochem Biotechnol. 2020; 193(3):896-911.

PMID: 33200269 DOI: 10.1007/s12010-020-03470-z.


Chlamydia trachomatis Oligopeptide Transporter Performs Dual Functions of Oligopeptide Transport and Peptidoglycan Recycling.

Singh R, Liechti G, Slade J, Maurelli A Infect Immun. 2020; 88(5).

PMID: 32094256 PMC: 7171251. DOI: 10.1128/IAI.00086-20.


References
1.
AMES G, Mimura C, Shyamala V . Bacterial periplasmic permeases belong to a family of transport proteins operating from Escherichia coli to human: Traffic ATPases. FEMS Microbiol Rev. 1990; 6(4):429-46. DOI: 10.1111/j.1574-6968.1990.tb04110.x. View

2.
Mourez M, Hofnung M, Dassa E . Subunit interactions in ABC transporters: a conserved sequence in hydrophobic membrane proteins of periplasmic permeases defines an important site of interaction with the ATPase subunits. EMBO J. 1997; 16(11):3066-77. PMC: 1169925. DOI: 10.1093/emboj/16.11.3066. View

3.
Sahm K, Matuschek M, Muller H, Mitchell W, Bahl H . Molecular analysis of the amy gene locus of Thermoanaerobacterium thermosulfurigenes EM1 encoding starch-degrading enzymes and a binding protein-dependent maltose transport system. J Bacteriol. 1996; 178(4):1039-46. PMC: 177763. DOI: 10.1128/jb.178.4.1039-1046.1996. View

4.
Singh R, Gradnigo J, White D, Lipzen A, Martin J, Schackwitz W . Complete Genome Sequence of an Evolved Thermotoga maritima Isolate. Genome Announc. 2015; 3(3). PMC: 4447916. DOI: 10.1128/genomeA.00557-15. View

5.
Chhabra S, Shockley K, Ward D, Kelly R . Regulation of endo-acting glycosyl hydrolases in the hyperthermophilic bacterium Thermotoga maritima grown on glucan- and mannan-based polysaccharides. Appl Environ Microbiol. 2002; 68(2):545-54. PMC: 126696. DOI: 10.1128/AEM.68.2.545-554.2002. View