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Different roles of DosS and DosT in the hypoxic adaptation of Mycobacteria.
- Source :
-
Journal of bacteriology [J Bacteriol] 2010 Oct; Vol. 192 (19), pp. 4868-75. Date of Electronic Publication: 2010 Jul 30. - Publication Year :
- 2010
-
Abstract
- The DosS (DevS) and DosT histidine kinases form a two-component system together with the DosR (DevR) response regulator in Mycobacterium tuberculosis. DosS and DosT, which have high sequence similarity to each other over the length of their amino acid sequences, contain two GAF domains (GAF-A and GAF-B) in their N-terminal sensory domains. Complementation tests in conjunction with phylogenetic analysis showed that DevS of Mycobacterium smegmatis is more closely related to DosT than DosS. We also demonstrated in vivo that DosS and DosT of M. tuberculosis play a differential role in hypoxic adaptation. DosT responds to a decrease in oxygen tension more sensitively and strongly than DosS, which might be attributable to their different autooxidation rates. The different responsiveness of DosS and DosT to hypoxia is due to the difference in their GAF-A domains accommodating the hemes. Multiple alignment analysis of the GAF-A domains of mycobacterial DosS (DosT) homologs and subsequent site-directed mutagenesis revealed that just one substitution of E87, D90, H97, L118, or T169 of DosS with the corresponding residue of DosT is sufficient to convert DosS to DosT with regard to the responsiveness to changes in oxygen tension.
- Subjects :
- Amino Acid Sequence
Bacterial Proteins classification
Bacterial Proteins genetics
Cell Hypoxia genetics
Cell Hypoxia physiology
Genetic Complementation Test
Models, Genetic
Molecular Sequence Data
Mutagenesis, Site-Directed
Mutation
Mycobacterium smegmatis genetics
Phylogeny
Protamine Kinase classification
Protamine Kinase genetics
Reverse Transcriptase Polymerase Chain Reaction
Sequence Homology, Amino Acid
Bacterial Proteins metabolism
Mycobacterium smegmatis metabolism
Protamine Kinase metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1098-5530
- Volume :
- 192
- Issue :
- 19
- Database :
- MEDLINE
- Journal :
- Journal of bacteriology
- Publication Type :
- Academic Journal
- Accession number :
- 20675480
- Full Text :
- https://doi.org/10.1128/JB.00550-10