Temporal transcriptomic response during arsenic stress in Herminiimonas arsenicoxydans
Open Access
- 17 December 2010
- journal article
- research article
- Published by Springer Science and Business Media LLC in BMC Genomics
- Vol. 11 (1), 709
- https://doi.org/10.1186/1471-2164-11-709
Abstract
Arsenic is present in numerous ecosystems and microorganisms have developed various mechanisms to live in such hostile environments. Herminiimonas arsenicoxydans, a bacterium isolated from arsenic contaminated sludge, has acquired remarkable capabilities to cope with arsenic. In particular our previous studies have suggested the existence of a temporal induction of arsenite oxidase, a key enzyme in arsenic metabolism, in the presence of As(III).Keywords
This publication has 35 references indexed in Scilit:
- Multiple controls affect arsenite oxidase gene expression in Herminiimonas arsenicoxydansBMC Microbiology, 2010
- The iron-sulfur clusters of dehydratases are primary intracellular targets of copper toxicityProceedings of the National Academy of Sciences of the United States of America, 2009
- Enhanced structural and functional genome elucidation of the arsenite-oxidizing strain Herminiimonas arsenicoxydans by proteomics dataBiochimie, 2009
- Cellular Defenses against Superoxide and Hydrogen PeroxideAnnual Review of Biochemistry, 2008
- Signaling mechanisms for activation of extracytoplasmic function (ECF) sigma factorsBiochimica et Biophysica Acta (BBA) - Biomembranes, 2007
- A Tale of Two Oxidation States: Bacterial Colonization of Arsenic-Rich EnvironmentsPLoS Genetics, 2007
- A Na + :H + Antiporter and a Molybdate Transporter Are Essential for Arsenite Oxidation in Agrobacterium tumefaciensJournal of Bacteriology, 2006
- Complex Regulation of Arsenite Oxidation in Agrobacterium tumefaciensJournal of Bacteriology, 2006
- Arsenite Oxidase aox Genes from a Metal-Resistant β-ProteobacteriumJournal of Bacteriology, 2003
- Crystal Structure of the 100 kDa Arsenite Oxidase from Alcaligenes faecalis in Two Crystal Forms at 1.64 Å and 2.03 ÅStructure, 2001