Cited by 719Tuberculosis Research and EpidemiologyBacterial Genetics and BiotechnologyMycobacterium research and diagnosis

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Rv3133c/ dosR is a transcription factor that mediates the hypoxic response of Mycobacterium tuberculosis

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Park, Heui‐Dong, Guinn, Kristi M., Harrell, Maria I., Liao, Reiling, Voskuil, Martin I., Tompa, Martin, Schoolnik, Gary K., Sherman, David R.·2003·Molecular Microbiology

DOI 10.1046/j.1365-2958.2003.03474.xPMC PMC1992516

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Abstract

Summary: Unlike many pathogens that are overtly harmful to their hosts, Mycobacterium tuberculosis can persist for years within humans in a clinically latent state. Latency is often linked to hypoxic conditions within the host. Among M. tuberculosis genes induced by hypoxia is a putative transcription factor, Rv3133c/DosR. We performed targeted disruption of this locus followed by transcriptome analysis of wild‐type and mutant bacilli. Nearly all the genes powerfully regulated by hypoxia require Rv3133c/DosR for their induction. Computer analysis identified a consensus motif, a variant of which is located upstream of nearly all M. tuberculosis genes rapidly induced by hypoxia. Further, Rv3133c/DosR binds to the two copies of this motif upstream of the hypoxic response gene alpha‐crystallin. Mutations within the binding sites abolish both Rv3133c/DosR binding as well as hypoxic induction of a downstream reporter gene. Also, mutation experiments with Rv3133c/DosR confirmed sequence‐based predictions that the C‐terminus is responsible for DNA binding and that the aspartate at position 54 is essential for function. Together, these results demonstrate that Rv3133c/DosR is a transcription factor of the two‐component response regulator class, and that it is the primary mediator of a hypoxic signal within M. tuberculosis .

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Molecular Cloning: A Laboratory Manual
Sambrook, J., Fritsch, E., & Maniatis, T. (1989) · UCLA - Biblioteca de Ciencias de la Salud · Cited by 133,589
Molecular cloning: A laboratory manual
Deininger, P. L. (1990) · Analytical Biochemistry · doi:10.1016/0003-2697(90)90595-z · Cited by 84,684
Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence
Cole, S. T., Brosch, R., Parkhill, J., Garnier, T., Churcher, C., Harris, D., Gordon, S. V., Eiglmeier, K., Gas, S., Barry, C. E., et al. (1998) · Nature · doi:10.1038/31159 · Cited by 7,847
Exploring the metabolic and genetic control of gene expression on a genomic scale.
Derisi, J., Iyer, V., & Brown, P. (1997) · Science · doi:10.1126/science.278.5338.680 · Cited by 4,832
Global Burden of Tuberculosis
Dye, C., Scheele, S., >Dolin, P., Pathania, V. S., Raviglione, M. C., & for the WHO Global Surveillance and Monitoring Project (1999) · JAMA · doi:10.1001/jama.282.7.677 · Cited by 2,955
Global Epidemiology of Tuberculosis
Raviglione, M. C. (1995) · JAMA · doi:10.1001/jama.273.3.220 · Cited by 1,754
COMMUNICATION MODULES IN BACTERIAL SIGNALING PROTEINS
Parkinson, J. S., & Kofoid, E. (1992) · Annual Review of Genetics · doi:10.1146/annurev.ge.26.120192.000443 · Cited by 1,450
Evaluation of a nutrient starvation model of Mycobacterium tuberculosis persistence by gene and protein expression profiling
Betts, J. C., Lukey, P. T., Robb, L. C., McAdam, R. A., & Duncan, K. (2002) · Molecular Microbiology · doi:10.1046/j.1365-2958.2002.02779.x · Cited by 1,395
Immunology of tuberculosis.
Flynn, J., & Chan, J. (2003) · Annual Review of Immunology · doi:10.1146/annurev.immunol.19.1.93 · Cited by 1,144
An in vitro model for sequential study of shiftdown of Mycobacterium tuberculosis through two stages of nonreplicating persistence
Wayne, L. G., & Hayes, L. G. (1996) · Infection and Immunity · doi:10.1128/iai.64.6.2062-2069.1996 · Cited by 1,141

Show all 61 references

Research works printed but not linked: 4

Ehrt S., 2002, Methods in Microbiology, 169
Enarson D.A., 1996, Tuberculosis, 55
Schoolnik G.K., 2001, Methods in Enzymology, 3
Yeager H.J., 1996, Tuberculosis, 363

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Das, J., Mapder, T., Chattopadhyay, S., & Banik, S. K. (2020) · PLoS ONE · doi:10.1371/journal.pone.0228967 · Cited by 3
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Priya, V. G. S., Bhandare, V. V., Muddapur, U. M., Swaminathan, P., Fandilolu, P. M., & Sonawane, K. D. (2020) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2020.1846620 · Cited by 3
Respiration and Oxidative Phosphorylation in Mycobacteria
Berney, M., & Cook, G. M. (2014) · Advances in photosynthesis and respiration · doi:10.1007/978-94-017-8742-0_15 · Cited by 3
The Sculpting of theMycobacterium tuberculosisGenome by Host Cell–Derived Pressures
Russell, D. G., Lee, W., Tan, S., Sukumar, N., Podinovskaia, M., Fahey, R. J., & VanderVen, B. C. (2014) · Microbiology Spectrum · doi:10.1128/microbiolspec.mgm2-0016-2013 · Cited by 3
Crystallization of a protein using dehydration without a precipitant
Sharpe, M. L., Baker, E. N., & Lott, J. S. (2005) · Acta Crystallographica Section F Structural Biology and Crystallization Communications · doi:10.1107/s1744309105014235 · Cited by 4
Statistics for clinicians. 5. Interval data (I).
Nanivadekar, A. S., & Kannappan, A. R. (1991) · PubMed · Cited by 3
SyNDI: synchronous network data integration framework
Lindfors, E., van Dam, J. C. J., Lam, C. M. C., Zondervan, N. A., dos Santos, V. A. P. M., & Diez, M. S. (2018) · BMC Bioinformatics · doi:10.1186/s12859-018-2426-5 · Cited by 3
DNA metabolism in mycobacteria
Warner, D. F. (2006) · University of the Witwatersrand, Johannesburg Institutional Repository on DSpace (University of the Witwatersrand, Johannesburg) · Cited by 3
TB Drug Discovery from Target Identification to Proof of Concept Studies
Dick, T., Dartois, V. A., Keller, T. H., & Matter, A. (2008) · Wiley eBooks · doi:10.1002/9783527611614.ch40 · Cited by 3
Resource misallocation as a mediator of fitness costs in antibiotic resistancePreprint
Trauner, A., Banaei‐Esfahani, A., Gygli, S. M., Warmer, P., Feldmann, J., Shafieechashmi, S., Eschbach, K., Zampieri, M., Borrell, S., Collins, B. C., et al. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/456434 · Cited by 3
An obligate aerobe adapts to hypoxia by hybridising fermentation with carbon storagePreprint
Gillett, D. L., Hutchinson, T. F., Mudaliyar, M., Watts, T. D., Wong, W. W., Locop, J., Jimenez, L., Hanchapola, I., Lee, H.-C., Tanuwidjaya, E., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.09.11.557286 · Cited by 3
Mycobacterium dormancy and antibiotic tolerance within the retinal pigment epithelium of ocular tuberculosis
Liu, R., Dang, J. N., Lee, R.-E., Lee, J. J., Kesavamoorthy, N., Ameri, H., Rao, N. A., & Eoh, H. (2024) · Microbiology Spectrum · doi:10.1128/spectrum.00788-24 · Cited by 3
Exploring the Protein Landscape of Dormant Mycobacterium tuberculosis Through In Vitro Functional Studies
Farnia, P., Velayati, A. A., Ghanavi, J., & Farnia, P. (2025) · Advances in experimental medicine and biology · doi:10.1007/978-3-031-96883-9_7 · Cited by 3
Systems analysis reveals alternate metabolic states adopted by Mycobacterium tuberculosis across species
Padilla‐Gómez, J., McGinn, R. A., Andrade, V., Liang, Y., Libby, K. A., Ni, H. M., Ringel, A. E., Evavold, C. L., & Bryson, B. D. (2026) · mSphere · doi:10.1128/msphere.00141-26 · Cited by 2
Mutational dynamics in Mycobacterium tuberculosis: implications for the evolution of drug resistance
Boshoff, H. I., Barry, C. E., & Mizrahi, V. (2004) · South African Journal of Science · Cited by 2
MSMEG_3955 from Mycobacterium smegmatis is a FMN bounded homotrimeric NAD(P)H:Flavin mononucleotide (FMN) oxidoreductase
Khosla, N., Thayil, S. M., Kaur, R., & Kesavan, A. K. (2021) · BMC Microbiology · doi:10.1186/s12866-021-02330-y · Cited by 2
M. tuberculosis PrrA binds the dosR promoter and regulates mycobacterial adaptation to hypoxia
Haller, Y. A., Jiang, J., Wan, Z., Childress, A., Wang, S., & Haydel, S. E. (2024) · Tuberculosis · doi:10.1016/j.tube.2024.102531 · Cited by 2
Regulation of Envelope Stress Responses byMycobacterium tuberculosis
Bretl, D. J., & Zahrt, T. C. (2016) · ASM Press eBooks · doi:10.1128/9781555818524.ch24 · Cited by 2
Solution structure of Rv0569, potent hypoxic signal transduction protein, from Mycobacterium tuberculosis
Kim, W.-J., Son, W. S., Ahn, D.-H., Im, H., Ahn, H., & Lee, B. (2013) · Tuberculosis · doi:10.1016/j.tube.2013.08.008 · Cited by 2
Mycobacterium tuberculosis: Strategies of offense and defense
Розов, С. М., & Дейнеко, Е. В. (2016) · Biology Bulletin Reviews · doi:10.1134/s2079086416040058 · Cited by 2
Efficient inference for sparse latent variable models of transcriptional regulation
Dai, Z., Iqbal, M., Lawrence, N. D., & Rattray, M. (2017) · Bioinformatics · doi:10.1093/bioinformatics/btx508 · Cited by 2
Host–Pathogen Interactions Influencing Mycobacterium tuberculosis Persistence and Drug Tolerance
Zheng, H., & Abramovitch, R. B. (2019) · Springer eBooks · doi:10.1007/978-3-030-25241-0_10 · Cited by 2
Transcription Factor Binding Site Mapping Using ChIP-Seq
Jaini, S., Lyubetskaya, A., Gomes, A. L. C., Peterson, M., Park, S. T., Raman, S., Schoolnik, G. K., & Galagan, J. E. (2015) · ASM Press eBooks · doi:10.1128/9781555818845.ch8 · Cited by 2
Self-citation
Drugs used in tuberculosis and leprosy
Swaminathan, S., & Rekha, V. V. B. (2009) · Side effects of drugs annual · doi:10.1016/s0378-6080(09)03130-4 · Cited by 2
Mycobacterium tuberculosis transcriptional regulator Rv1019 is upregulated in hypoxia, and negatively regulates Rv3230c‐Rv3229c operon encoding enzymes in the oleic acid biosynthetic pathway
Pushparajan, A. R., Edison, L. K., & Kumar, R. A. (2022) · FEBS Journal · doi:10.1111/febs.16647 · Cited by 2

Authors: Park, H., Guinn, K. M., Harrell, M. I., Liao, R., Voskuil, M. I., Tompa, M., Schoolnik, G. K., & Sherman, D. R.
Affiliations: University of Washington (US)
Stanford Medicine (US)
Corresponding author: Sherman, David R.
ORCID: Voskuil, Martin I.
Sherman, David R.
Venue: Molecular Microbiology
Publisher: Wiley
Published: 2003-04-09
Volume: 48
Issue: 3
Pages: 833-843
ISSN: 0950-382X (ISSN-L)
1365-2958
DOI: 10.1046/j.1365-2958.2003.03474.x
PMC: PMC1992516
OpenAlex: W2120842435
Cited by: 712
References: 61
Citations by year: 2026: 20 · 2025: 22 · 2024: 20 · 2023: 26 · 2022: 24 · 2021: 37 · 2020: 34 · 2019: 35 · 2018: 28 · 2017: 33 · 2016: 30 · 2015: 31 · 2014: 46 · 2013: 32 · 2012: 41
FWCI: 14.66
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: onlinelibrary.wiley.com/termsAndConditions#vor (vor)
Locations: Molecular Microbiology (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
Funders: National Science Foundation (9974498)
National Institutes of Health
National Human Genome Research Institute (HG02602-01, R01HG002602)
National Institute of Allergy and Infectious Diseases (R01AI044826, AI-44826, R21AI047744, AI47744, R01AI047744)
Topics: Health Sciences › Medicine › Infectious Diseases › Tuberculosis Research and Epidemiology
Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
Health Sciences › Medicine › Epidemiology › Mycobacterium research and diagnosis
Keywords: Mycobacterium tuberculosis, transcription factors, hypoxia response, hypoxia, transcriptional regulation, two-component response regulator, DNA-binding motifs, alpha-crystallin, latent tuberculosis infection, gene induction
MeSH terms: Hypoxia, Aspartic Acid, Bacterial Proteins, Humans, Mycobacterium tuberculosis, Oxygen, Protein Binding, Regulatory Sequences, Nucleic Acid, Transcription Factors, Tuberculosis, Gene Expression Regulation, Bacterial, Genes, Reporter, Gene Targeting, Oligonucleotide Array Sequence Analysis

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Rv3133c/ dosR is a transcription factor that mediates the hypoxic response of Mycobacterium tuberculosis

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