Structures of Mycobacterium tuberculosis DosR and DosR-DNA Complex Involved in Gene Activation during Adaptation to Hypoxic Latency
Abstract
On encountering low oxygen conditions, DosR activates the transcription of 47 genes, promoting long-term survival of Mycobacterium tuberculosis in a non-replicating state. Here, we report the crystal structures of the DosR C-terminal domain and its complex with a consensus DNA sequence of the hypoxia-induced gene promoter. The DosR C-terminal domain contains four {alpha}-helices and forms tetramers consisting of two dimers with non-intersecting dyads. In the DNA-bound structure, each DosR C-terminal domain in a dimer places its DNA-binding helix deep into the major groove, causing two bends in the DNA. DosR makes numerous protein-DNA base contacts using only three amino acid residues per subunit: Lys179, Lys182, and Asn183. The DosR tetramer is unique among response regulators with known structures.
- Authors:
-
- UWASH
- Publication Date:
- Research Org.:
- Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
- Sponsoring Org.:
- USDOE
- OSTI Identifier:
- 1008668
- Resource Type:
- Journal Article
- Journal Name:
- Journal of Molecular Biology
- Additional Journal Information:
- Journal Volume: 354; Journal Issue: (3) ; 2005; Journal ID: ISSN 0022-2836
- Publisher:
- Elsevier
- Country of Publication:
- United States
- Language:
- ENGLISH
- Subject:
- 36 MATERIALS SCIENCE; AMINO ACIDS; CRYSTAL STRUCTURE; DIMERS; DNA; GENES; MYCOBACTERIUM TUBERCULOSIS; OXYGEN; RESIDUES; TRANSCRIPTION; TUBERCULOSIS
Citation Formats
Wisedchaisri, Goragot, Wu, Meiting, Rice, Adrian E, Roberts, David M, Sherman, David R, and Hol, Wim G.J. Structures of Mycobacterium tuberculosis DosR and DosR-DNA Complex Involved in Gene Activation during Adaptation to Hypoxic Latency. United States: N. p., 2010.
Web. doi:10.1016/j.jmb.2005.09.048.
Wisedchaisri, Goragot, Wu, Meiting, Rice, Adrian E, Roberts, David M, Sherman, David R, & Hol, Wim G.J. Structures of Mycobacterium tuberculosis DosR and DosR-DNA Complex Involved in Gene Activation during Adaptation to Hypoxic Latency. United States. https://doi.org/10.1016/j.jmb.2005.09.048
Wisedchaisri, Goragot, Wu, Meiting, Rice, Adrian E, Roberts, David M, Sherman, David R, and Hol, Wim G.J. 2010.
"Structures of Mycobacterium tuberculosis DosR and DosR-DNA Complex Involved in Gene Activation during Adaptation to Hypoxic Latency". United States. https://doi.org/10.1016/j.jmb.2005.09.048.
@article{osti_1008668,
title = {Structures of Mycobacterium tuberculosis DosR and DosR-DNA Complex Involved in Gene Activation during Adaptation to Hypoxic Latency},
author = {Wisedchaisri, Goragot and Wu, Meiting and Rice, Adrian E and Roberts, David M and Sherman, David R and Hol, Wim G.J.},
abstractNote = {On encountering low oxygen conditions, DosR activates the transcription of 47 genes, promoting long-term survival of Mycobacterium tuberculosis in a non-replicating state. Here, we report the crystal structures of the DosR C-terminal domain and its complex with a consensus DNA sequence of the hypoxia-induced gene promoter. The DosR C-terminal domain contains four {alpha}-helices and forms tetramers consisting of two dimers with non-intersecting dyads. In the DNA-bound structure, each DosR C-terminal domain in a dimer places its DNA-binding helix deep into the major groove, causing two bends in the DNA. DosR makes numerous protein-DNA base contacts using only three amino acid residues per subunit: Lys179, Lys182, and Asn183. The DosR tetramer is unique among response regulators with known structures.},
doi = {10.1016/j.jmb.2005.09.048},
url = {https://www.osti.gov/biblio/1008668},
journal = {Journal of Molecular Biology},
issn = {0022-2836},
number = (3) ; 2005,
volume = 354,
place = {United States},
year = {Tue Jul 20 00:00:00 EDT 2010},
month = {Tue Jul 20 00:00:00 EDT 2010}
}