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Ha-Na Lee 2 Articles
Mycobacterial Regulatory Systems Involved in the Regulation of Gene Expression Under Respiration‑Inhibitory Conditions
Yuna Oh , Ha-Na Lee , Eon-Min Ko , Ji-A Jeong , Sae Woong Park , Jeong-Il Oh
J. Microbiol. 2023;61(3):297-315.   Published online February 27, 2023
DOI: https://doi.org/10.1007/s12275-023-00026-8
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  • 4 Web of Science
  • 4 Crossref
AbstractAbstract PDF
Mycobacterium tuberculosis is the causative agent of tuberculosis. M. tuberculosis can survive in a dormant state within the granuloma, avoiding the host-mounting immune attack. M. tuberculosis bacilli in this state show increased tolerance to antibiotics and stress conditions, and thus the transition of M. tuberculosis to the nonreplicating dormant state acts as an obstacle to tuberculosis treatment. M. tuberculosis in the granuloma encounters hostile environments such as hypoxia, nitric oxide, reactive oxygen species, low pH, and nutrient deprivation, etc., which are expected to inhibit respiration of M. tuberculosis. To adapt to and survive in respiration-inhibitory conditions, it is required for M. tuberculosis to reprogram its metabolism and physiology. In order to get clues to the mechanism underlying the entry of M. tuberculosis to the dormant state, it is important to understand the mycobacterial regulatory systems that are involved in the regulation of gene expression in response to respiration inhibition. In this review, we briefly summarize the information regarding the regulatory systems implicated in upregulation of gene expression in mycobacteria exposed to respiration-inhibitory conditions. The regulatory systems covered in this review encompass the DosSR (DevSR) two-component system, SigF partner switching system, MprBA-SigE-SigB signaling pathway, cAMP receptor protein, and stringent response.

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Citations to this article as recorded by  
  • Genetic and immunologic determinants of BCG disease: from mechanism to prevention
    Feng Chen, Yifan Shen, Qianhui Yan, Daishan Zheng, Xiaoli Chen, Longyu Fang, Mengchen Sun, Yuansi Zhang, Maoping Chu, Enhui Yang, Xiu-Feng Huang
    Annals of Medicine.2026;[Epub]     CrossRef
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    Ming-Rui Sun, Jia-Yin Xing, Xiao-Tian Li, Ren Fang, Yang Zhang, Zhao-Li Li, Ning-Ning Song
    Journal of Microbiology, Immunology and Infection.2025; 58(5): 497.     CrossRef
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    Eun-Jin Park, Insoo Kim, Eun-Kyeong Jo
    Journal of Bacteriology and Virology.2024; 54(3): 167.     CrossRef
  • Bacterial Regulatory Mechanisms for the Control of Cellular Processes: Simple Organisms’ Complex Regulation
    Jin-Won Lee
    Journal of Microbiology.2023; 61(3): 273.     CrossRef
Protein-Protein Interactions between Histidine Kinases and Response Regulators of Mycobacterium tuberculosis H37Rv
Ha-Na Lee , Kwang-Eun Jung , In-Jeong Ko , Hyung Suk Baik , Jeong-Il Oh
J. Microbiol. 2012;50(2):270-277.   Published online April 27, 2012
DOI: https://doi.org/10.1007/s12275-012-2050-4
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  • 25 Crossref
AbstractAbstract PDF
Using yeast two-hybrid assay, we investigated protein-protein interactions between all orthologous histidine kinase (HK)/response regulator (RR) pairs of M. tuberculosis H37Rv and identified potential protein-protein interactions between a noncognate HK/RR pair, DosT/NarL. The protein interaction between DosT and NarL was verified by phosphotransfer reaction from DosT to NarL. Furthermore, we found that the DosT and DosS HKs, which share considerable sequence similarities to each other and form a twocomponent system with the DosR RR, have different crossinteraction capabilities with NarL: DosT interacted with NarL, while DosS did not. The dimerization domains of DosT and DosS were shown to be sufficient to confer specificity for DosR, and the different cross-interaction abilities of DosS and DosT with NarL were demonstrated to be attributable to variations in the amino acid sequences of the α2-helices of their dimerization domains.

Citations

Citations to this article as recorded by  
  • Multiple input–multiple output (MIMO) designs in two-component signalling systems of Mycobacterium tuberculosis
    Devendra Pratap Singh, Gayathri A S, Ramandeep Singh, Narendra M Dixit, Deepak Kumar Saini, Michael Bott
    FEMS Microbiology Reviews.2026;[Epub]     CrossRef
  • Activation of the MprBA two-component system in Mycobacterium smegmatis under acidic and respiration-inhibitory conditions and crosstalk between MprA and KdpD
    Yun-Kyung Kim, Ye-Jin Lee, Jeong-Il Oh, Patricia A. Champion
    Journal of Bacteriology.2026;[Epub]     CrossRef
  • Harnessing hypoxia: bacterial adaptation and chronic infection in cystic fibrosis
    Ciarán J Carey, Niamh Duggan, Joanna Drabinska, Siobhán McClean
    FEMS Microbiology Reviews.2025;[Epub]     CrossRef
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    Prabhat Ranjan Singh, Harsh Goar, Partha Paul, Khushboo Mehta, Bhanwar Bamniya, Anil Kumar Vijjamarri, Roohi Bansal, Hina Khan, Subramanian Karthikeyan, Dibyendu Sarkar, Danielle A. Garsin
    PLOS Genetics.2023; 19(12): e1011070.     CrossRef
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    Zilu Wang, Jianping Xie
    Cellular Signalling.2022; 91: 110238.     CrossRef
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    David Giacalone, Rochelle E. Yap, Alwyn M. V. Ecker, Shumin Tan, Danielle A. Garsin
    PLOS Genetics.2022; 18(8): e1010331.     CrossRef
  • Sensing of O2 and nitrate by bacteria: alternative strategies for transcriptional regulation of nitrate respiration by O2 and nitrate
    Gottfried Unden, Robin Klein
    Environmental Microbiology.2021; 23(1): 5.     CrossRef
  • Nitrate-nitrite fate and oxygen sensing in dormant Mycobacterium tuberculosis: A bioinorganic approach highlighting the importance of transition metals
    Eduardo H.S. Sousa, Marta S.P. Carepo, José J.G. Moura
    Coordination Chemistry Reviews.2020; 423: 213476.     CrossRef
  • Inhibiting Mycobacterium tuberculosis DosRST Signaling by Targeting Response Regulator DNA Binding and Sensor Kinase Heme
    Huiqing Zheng, John T. Williams, Bilal Aleiwi, Edmund Ellsworth, Robert B. Abramovitch
    ACS Chemical Biology.2020; 15(1): 52.     CrossRef
  • Acetylation of Response Regulator Proteins, TcrX and MtrA in M. tuberculosis Tunes their Phosphotransfer Ability and Modulates Two-Component Signaling Crosstalk
    Krishna Kumar Singh, Neerupma Bhardwaj, Gaurav D. Sankhe, Niveda Udaykumar, Rambir Singh, Vandana Malhotra, Deepak Kumar Saini
    Journal of Molecular Biology.2019; 431(4): 777.     CrossRef
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    Romain Veyron-Churlet, Camille Locht
    Pathogens.2019; 8(4): 173.     CrossRef
  • Dual control of RegX3 transcriptional activity by SenX3 and PknB
    Eun-Jin Park, Yu-Mi Kwon, Jin-Won Lee, Ho-Young Kang, Jeong-Il Oh
    Journal of Biological Chemistry.2019; 294(28): 11023.     CrossRef
  • Oxygen triggers signal transduction in the DevS (DosS) sensor of Mycobacterium tuberculosis by modulating the quaternary structure
    Josiane Bezerra da Silva Lobão, Ana C. S. Gondim, Wellinson G. Guimarães, Marie‐Alda Gilles‐Gonzalez, Luiz Gonzaga de França Lopes, Eduardo H. S. Sousa
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    International Journal of Molecular Sciences.2018; 19(2): 347.     CrossRef
  • Inhibition of the DevSR Two-Component System by Overexpression of Mycobacterium tuberculosis PknB in Mycobacterium smegmatis
    Hyun-Jung Bae, Ha-Na Lee, Mi-Na Baek, Eun-Jin Park, Chi-Yong Eom, In-Jeong Ko, Ho-Young Kang, Jeong-Il Oh
    Molecules and Cells.2017; 40(9): 632.     CrossRef
  • The two-component signalling networks of Mycobacterium tuberculosis display extensive cross-talk in vitro
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  • Phylogenomics of Mycobacterium Nitrate Reductase Operon
    Qinqin Huang, Abualgasim Elgaili Abdalla, Jianping Xie
    Current Microbiology.2015; 71(1): 121.     CrossRef
  • Genome-wide prediction of prokaryotic two-component system networks using a sequence-based meta-predictor
    Altan Kara, Martin Vickers, Martin Swain, David E. Whitworth, Narcis Fernandez-Fuentes
    BMC Bioinformatics.2015;[Epub]     CrossRef
  • Two-Component Regulatory Systems of Mycobacteria
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    Microbiology Spectrum.2014;[Epub]     CrossRef
  • Rv1027c–Rv1028c encode functional KdpDE two – Component system in Mycobacterium tuberculosis
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    Biochemical and Biophysical Research Communications.2014; 446(4): 1172.     CrossRef
  • Serine 83 in DosR, a response regulator from Mycobacterium tuberculosis, promotes its transition from an activated, phosphorylated state to an inactive, unphosphorylated state
    Ha Yeon Cho, Beom Sik Kang
    Biochemical and Biophysical Research Communications.2014; 444(4): 651.     CrossRef
  • Proteome and phosphoproteome analysis of the serine/threonine protein kinase E mutant of Mycobacterium tuberculosis
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    Expert Review of Proteomics.2014; 11(6): 745.     CrossRef
  • Involvement of the catalytically important Asp54 residue ofMycobacterium smegmatisDevR in protein-protein interactions between DevR and DevS
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    FEMS Microbiology Letters.2013; 343(1): 26.     CrossRef

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