Journal of Microbiology

Jeong-Il Oh

8 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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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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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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Bacterial Regulatory Mechanisms for the Control of Cellular Processes: Simple Organisms’ Complex Regulation
Jin-Won Lee
Journal of Microbiology.2023; 61(3): 273. CrossRef

Negative regulation of the acsA1 gene encoding the major acetyl-CoA synthetase by cAMP receptor protein in Mycobacterium smegmatis: Eon-Min Ko , Yuna Oh , Jeong-Il Oh; J. Microbiol. 2022;60(12):1139-1152. Published online October 24, 2022; DOI: https://doi.org/10.1007/s12275-022-2347-x

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Acetyl-CoA synthetase (ACS) is the enzyme that irreversibly catalyzes the synthesis of acetyl-CoA from acetate, CoA-SH, and ATP via acetyl-AMP as an intermediate. In this study, we demonstrated that AcsA1 (MSMEG_6179) is the predominantly expressed ACS among four ACSs (MSMEG_6179, MSMEG_0718, MSMEG_3986, and MSMEG_5650) found in Mycobacterium smegmatis and that a deletion mutation of acsA1 in M. smegmatis led to its compromised growth on acetate as the sole carbon source. Expression of acsA1 was demonstrated to be induced during growth on acetate as the sole carbon source. The acsA1 gene was shown to be negatively regulated by Crp1 (MSMEG_6189) that is the major cAMP receptor protein (CRP) in M. smegmatis. Using DNase I footprinting analysis and site-directed mutagenesis, a CRPbinding site (GGTGA-N6-TCACA) was identified in the upstream regulatory region of acsA1, which is important for repression of acsA1 expression. We also demonstrated that inhibition of the respiratory electron transport chain by inactivation of the major terminal oxidase, aa3 cytochrome c oxidase, led to a decrease in acsA1 expression probably through the activation of CRP. In conclusion, AcsA1 is the major ACS in M. smegmatis and its gene is under the negative regulation of Crp1, which contributes to some extent to the induction of acsA1 expression under acetate conditions. The growth of M. smegmatis is severely impaired on acetate as the sole carbon source under respiration-inhibitory conditions.

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Microbial acetyl-CoA synthesis as an emerging metabolic and regulatory hub in plant-microbe interactions
Yanan Zhou, Xue-Xian Zhang, Dandan Wang, Mengguang Zhao, Li Sun, Weiwei Huang, Zhihong Xie
Microbiological Research.2026; 304: 128413. CrossRef
Inhibitory activity and antioomycete mechanism of citral against Phytophthora capsici
Kaidi Cui, Yinan Wang, Mengke Wang, Te Zhao, Fulong Zhang, Leiming He, Lin Zhou
Pesticide Biochemistry and Physiology.2024; 204: 106067. CrossRef
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
Journal of Microbiology.2023; 61(3): 297. CrossRef

Activation of the SigE-SigB signaling pathway by inhibition of the respiratory electron transport chain and its effect on rifampicin resistance in Mycobacterium smegmatis: Yuna Oh , Hye-In Lee , Ji-A Jeong , Seonghan Kim , Jeong-Il Oh; J. Microbiol. 2022;60(9):935-947. Published online August 1, 2022; DOI: https://doi.org/10.1007/s12275-022-2202-0

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Using a mutant of Mycobacterium smegmatis lacking the major aa3 cytochrome c oxidase of the electron transport chain (Δaa3), we demonstrated that inhibition of the respiratory electron transport chain led to an increase in antibiotic resistance of M. smegmatis to isoniazid, rifampicin, ethambutol, and tetracycline. The alternative sigma factors SigB and SigE were shown to be involved in an increase in rifampicin resistance of M. smegmatis induced under respiration-inhibitory conditions. As in Mycobacterium tuberculosis, SigE and SigB form a hierarchical regulatory pathway in M. smegmatis through SigE-dependent transcription of sigB. Expression of sigB and sigE was demonstrated to increase in the Δaa3 mutant, leading to upregulation of the SigB-dependent genes in the mutant. The phoU2 (MSMEG_1605) gene implicated in a phosphatesignaling pathway and the MSMEG_1097 gene encoding a putative glycosyltransferase were identified to be involved in the SigB-dependent enhancement of rifampicin resistance observed for the Δaa3 mutant of M. smegmatis. The significance of this study is that the direct link between the functionality of the respiratory electron transport chain and antibiotic resistance in mycobacteria was demonstrated for the first time using an electron transport chain mutant rather than inhibitors of electron transport chain.

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Yaqi Cui, Ruilin Lou, Zulpya Mahmut, Fangyu Shi, Jiaqi Zhou, Yaqi Zhu, Zhenzhou Wang, Yifan Chen, Lin Xu, Lin Wang, Biao Dong
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Mo(SO)2 porous nanoparticles achieve effective antibacterial through electron attack on the respiratory chain
Yaqi Cui, Zulpya Mahmut, Yangdong Xie, Fangyu Shi, Jiaqi Zhou, Yaqi Zhu, Ruilin Lou, Zhenzhou Wang, Lin Xu, Lin Wang, Biao Dong
Chemical Engineering Journal.2026; 529: 172994. CrossRef
Regulatory mechanism of the SenX3-RegX3 two-component system in Mycobacterium smegmatis: Roles of PhoU in sensing inorganic phosphate levels
Youjin Seung, Ha-Eun Baik, Eun-Jin Park, Jeong-Il Oh
Journal of Biological Chemistry.2025; 301(8): 110435. CrossRef
Inactivation of cAMP receptor protein (MSMEG_6189) increases isoniazid susceptibility in Mycobacterium smegmatis via altered oxidative phosphorylation, elevated ROS production, and loss of ahpC
Narin Kim, Yuna Oh, Jeong-Il Oh, Tina M. Henkin
Journal of Bacteriology.2025;[Epub] CrossRef
Rel-dependent decrease in the expression of ribosomal protein genes by inhibition of the respiratory electron transport chain in Mycobacterium smegmatis
Na-Kyeong Kim, Jong-Eun Baek, Ye-Jin Lee, Yuna Oh, Jeong-Il Oh
Frontiers in Microbiology.2024;[Epub] CrossRef
MoaB2, a newly identified transcription factor, binds to σ A in Mycobacterium smegmatis
Barbora Brezovská, Subhash Narasimhan, Michaela Šiková, Hana Šanderová, Tomáš Kovaľ, Nabajyoti Borah, Mahmoud Shoman, Debora Pospíšilová, Viola Vaňková Hausnerová, Dávid Tužinčin, Martin Černý, Jan Komárek, Martina Janoušková, Milada Kambová, Petr Halada,
Journal of Bacteriology.2024;[Epub] CrossRef
Enhanced hypoxanthine utilization for cAMP salvage synthesis efficiently by Arthrobacter sp. CCTCC 2013431 via xanthine oxidase inhibition
Baofeng Chen, Hai Tan, Chang Li, Linbo Li, Zhonghua Zhang, Zhigang Li
Biotechnology Letters.2024; 46(6): 1095. CrossRef
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
Journal of Microbiology.2023; 61(3): 297. CrossRef

Functional characterization of HigBA toxin-antitoxin system in an Arctic bacterium, Bosea sp. PAMC 26642: Eunsil Choi , Ahhyun Huh , Changmin Oh , Jeong-Il Oh , Ho Young Kang , Jihwan Hwang; J. Microbiol. 2022;60(2):192-206. Published online February 1, 2022; DOI: https://doi.org/10.1007/s12275-022-1619-9

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Toxin-antitoxin (TA) systems are growth-controlling genetic elements consisting of an intracellular toxin protein and its cognate antitoxin. TA systems have been spread among microbial genomes through horizontal gene transfer and are now prevalent in most bacterial and archaeal genomes. Under normal growth conditions, antitoxins tightly counteract the activity of the toxins. Upon stresses, antitoxins are inactivated, releasing activated toxins, which induce growth arrest or cell death. In this study, among nine functional TA modules in Bosea sp. PAMC 26642 living in Arctic lichen, we investigated the functionality of BoHigBA2. BohigBA2 is located close to a genomic island and adjacent to flagellar gene clusters. The expression of BohigB2 induced the inhibition of E. coli growth at 37°C, which was more manifest at 18°C, and this growth defect was reversed when BohigA2 was co-expressed, suggesting that this BoHigBA2 module might be an active TA module in Bosea sp. PAMC 26642. Live/dead staining and viable count analyses revealed that the BoHigB2 toxin had a bactericidal effect, causing cell death. Furthermore, we demonstrated that BoHigB2 possessed mRNA-specific ribonuclease activity on various mRNAs and cleaved only mRNAs being translated, which might impede overall translation and consequently lead to cell death. Our study provides the insight to understand the cold adaptation of Bosea sp. PAMC 26642 living in the Arctic.

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Evaluating the Contribution of the Predicted Toxin–Antitoxin System HigBA to Persistence, Biofilm Formation, and Virulence in Burkholderia pseudomallei
Itziar Chapartegui-González, Nittaya Khakhum, Jacob L. Stockton, Alfredo G. Torres, Igor E. Brodsky
Infection and Immunity.2022;[Epub] CrossRef
Chronicle of Research into Lichen-Associated Bacteria
Zichen He, Takeshi Naganuma
Microorganisms.2022; 10(11): 2111. CrossRef
Degradation of amoxicillin by newly isolated Bosea sp. Ads-6
Lei Yan, Ning Yan, Xi-Yan Gao, Ying Liu, Zhi-Pei Liu
Science of The Total Environment.2022; 828: 154411. CrossRef

Alanine dehydrogenases in mycobacteria: Ji-A Jeong , Jeong-Il Oh; J. Microbiol. 2019;57(2):81-92. Published online January 31, 2019; DOI: https://doi.org/10.1007/s12275-019-8543-7

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Since NAD(H)-dependent L-alanine dehydrogenase (EC 1.1.4.1; Ald) was identified as one of the major antigens present in culture filtrates of Mycobacterium tuberculosis, many studies on the enzyme have been conducted. Ald catalyzes the reversible conversion of pyruvate to alanine with concomitant oxidation of NADH to NAD+ and has a homohexameric quaternary structure. Expression of the ald genes was observed to be strongly upregulated in M. tuberculosis and Mycobacterium smegmatis grown in the presence of alanine. Furthermore, expression of the ald genes in some mycobacteria was observed to increase under respiration-inhibitory conditions such as oxygen-limiting and nutrient-starvation conditions. Upregulation of ald expression by alanine or under respiration-inhibitory conditions is mediated by AldR, a member of the Lrp/AsnC family of transcriptional regulators. Mycobacterial Alds were demonstrated to be the enzymes required for utilization of alanine as a nitrogen source and to help mycobacteria survive under respiration-inhibitory conditions by maintaining cellular NADH/NAD+ homeostasis. Several inhibitors of Ald have been developed, and their application in combination with respiration-inhibitory antitubercular drugs such as Q203 and bedaquiline was recently suggested.

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Functional characterization of the cutI gene for the transcription of carbon monoxide dehydrogenase genes in Mycobacterium sp. strain JC1 DSM 3803: Jae Ho Lee , Sae Woong Park , Young Min Kim , Jeong-Il Oh; J. Microbiol. 2017;55(1):31-36. Published online December 30, 2016; DOI: https://doi.org/10.1007/s12275-017-6572-7

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Carbon monoxide dehydrogenase (CO-DH) in Mycobacterium sp. strain JC1 is a key enzyme for the carboxydotrophic growth, when carbon monoxide (CO) is supplied as a sole source of carbon and energy. This enzyme is also known to act as nitric oxide dehydrogenase (NO-DH) for the detoxification of NO. Several accessory genes such as cutD, cutE, cutF, cutG, cutH, and cutI, are clustered together with two copies of the CO-DH structural genes (cutB1C1A1 and cutB2C2A2) in Mycobacterium sp. strain JC1 and are well conserved in carboxydotrophic mycobacteria. Transcription of the CO-DH structural and accessory genes was demonstrated to be increased significantly by acidified sodium nitrate as a source of NO. A cutI deletion (ΔcutI) mutant of Mycobacterium sp. strain JC1 was generated to identity the function of CutI. Lithoautotrophic growth of the ΔcutI mutant was severely affected in mineral medium supplemented with CO, while the mutant grew normally with glucose. Western blotting, CO-DH activity staining, and CO-DH-specific enzyme assay revealed a significant decrease in the cellular level of CO-DH in the ΔcutI mutant. Northern blot analysis and promoter assay showed that expression of the cutB1 and cutB2 genes was significantly reduced at the transcriptional level in the ΔcutI mutant, compared to that of the wildtype strain. The ΔcutI mutant was much more susceptible to NO than was the wild type.

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Characterization of a MHYT domain-coupled transcriptional regulator that responds to carbon monoxide
Gonzalo Durante-Rodríguez, Sofía de Francisco-Polanco, José Luis García, Eduardo Díaz
Nucleic Acids Research.2024; 52(15): 8849. CrossRef
Molybdenum Enzymes and How They Support Virulence in Pathogenic Bacteria
Qifeng Zhong, Bostjan Kobe, Ulrike Kappler
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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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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.

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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
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Effect of Mutations of Five Conserved Histidine Residues in the Catalytic Subunit of the cbb3 Cytochrome c Oxidase on its Function: Jeong-Il Oh; J. Microbiol. 2006;44(3):284-292.; DOI: https://doi.org/2384 [pii]

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Abstract PDF: The cbb3 cytochrome c oxidase has the dual function as a terminal oxidase and oxygen sensor in the photosynthetic bacterium, Rhodobacter sphaeroides. The cbb3 oxidase forms a signal transduction pathway together with the PrrBA two-component system that controls photosynthesis gene expression in response to changes in oxygen tension in the environment. Under aerobic conditions the cbb3 oxidase generates an inhibitory signal, which shifts the equilibrium of PrrB kinase/phosphatase activities towards the phosphatase mode. Photosynthesis genes are thereby turned off under aerobic conditions. The catalytic subunit (CcoN) of the R. sphaeroides cbb3 oxidase contains five histidine residues (H214, H233, H303, H320, and H444) that are conserved in all CcoN subunits of the cbb3 oxidase, but not in the catalytic subunits of other members of copper-heme superfamily oxidases. H214A mutation of CcoN affected neither catalytic activity nor sensory (signaling) function of the cbb3 oxidase, whereas H320A mutation led to almost complete loss of both catalytic activity and sensory function of the cbb3 oxidase. H233V and H444A mutations brought about the partial loss of catalytic activity and sensory function of the cbb3 oxidase. Interestingly, the H303A mutant form of the cbb3 oxidase retains the catalytic function as a cytochrome c oxidase as compared to the wild-type oxidase, while it is defective in signaling function as an oxygen sensor. H303 appears to be implicated in either signal sensing or generation of the inhibitory signal to the PrrBA two-component system.

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