The F 1 F o -ATP Synthase of Mycobacterium smegmatis Is Essential for Growth
- 1 July 2005
- journal article
- research article
- Published by American Society for Microbiology in Journal of Bacteriology
- Vol. 187 (14), 5023-5028
- https://doi.org/10.1128/jb.187.14.5023-5028.2005
Abstract
The F1Fo-ATP synthase plays an important role in a number of vital cellular processes in plants, animals, and microorganisms. In this study, we constructed a ΔatpD mutant of Mycobacterium smegmatis and demonstrated that atpD encoding the β subunit of the F1Fo-ATP synthase is an essential gene in M. smegmatis during growth on nonfermentable and fermentable carbon sources.Keywords
This publication has 37 references indexed in Scilit:
- Mutants of Mycobacterium smegmatis unable to grow at acidic pH in the presence of the protonophore carbonyl cyanide m-chlorophenylhydrazoneMicrobiology, 2005
- Altered NADH/NAD + Ratio Mediates Coresistance to Isoniazid and Ethionamide in MycobacteriaAntimicrobial Agents and Chemotherapy, 2005
- A Diarylquinoline Drug Active on the ATP Synthase of Mycobacterium tuberculosisScience, 2005
- Replacement of Amino Acid Sequence Features of a- and c-Subunits of ATP Synthases of Alkaliphilic Bacillus with the Bacillus Consensus Sequence Results in Defective Oxidative Phosphorylation and Non-fermentative Growth at pH 10.5Journal of Biological Chemistry, 2004
- Surviving the Acid Test: Responses of Gram-Positive Bacteria to Low pHMicrobiology and Molecular Biology Reviews, 2003
- Introduction of a Carboxyl Group in the First Transmembrane Helix ofEscherichia coliF1FoATPase Subunitcand Cytoplasmic pH RegulationJournal of Bacteriology, 2001
- Analysis of the role of the Listeria monocytogenes F0F1-ATPase operon in the acid tolerance responseInternational Journal of Food Microbiology, 2000
- Growth ofMycobacterium tuberculosisin a Defined Medium Is Very Restricted by Acid pH and Mg2+LevelsInfection and Immunity, 2000
- THE ATP SYNTHASE—A SPLENDID MOLECULAR MACHINEAnnual Review of Biochemistry, 1997
- Isolation and characterization of efficient plasmid transformation mutants of Mycobacterium smegmatisMolecular Microbiology, 1990