- Mycobacterial Regulatory Systems Involved in the Regulation of Gene Expression Under Respiration‑Inhibitory Conditions
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Yuna Oh , Ha-Na Lee , Eon-Min Ko , Ji-A Jeong , Sae Woong Park , Jeong-Il Oh
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J. Microbiol. 2023;61(3):297-315. Published online February 27, 2023
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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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Citations
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- Protein-Protein Interactions between Histidine Kinases and Response Regulators of Mycobacterium tuberculosis H37Rv
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Ha-Na Lee , Kwang-Eun Jung , In-Jeong Ko , Hyung Suk Baik , Jeong-Il Oh
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J. Microbiol. 2012;50(2):270-277. Published online April 27, 2012
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DOI: https://doi.org/10.1007/s12275-012-2050-4
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794
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Abstract
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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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