Review
- 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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Abstract
- 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.
Journal Articles
- Propionate, together with triple antibiotics, inhibits the growth of Enterococci
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Soyoung Jeong , Yunjae Lee , Cheol-Heui Yun , Ok-Jin Park , Seung Hyun Han
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J. Microbiol. 2019;57(11):1019-1024. Published online October 28, 2019
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DOI: https://doi.org/10.1007/s12275-019-9434-7
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Abstract
- Enterococci are Gram-positive facultative anaerobic bacteria
that colonize the oral cavity and gastrointestinal tract. Enterococcal
infections, mainly caused by Enterococcus faecalis
and Enterococcus faecium, include apical periodontitis, endocarditis,
and bloodstream infections. Recently, vancomycinresistant
Enterococci are considered major pathogens that
are common but difficult to treat, especially in nosocomial
settings. Moreover, E. faecalis is closely associated with recurrent
endodontic infections and failed endodontic treatment.
In this study, we investigated the effects of short-chain
fatty acids (SCFAs), acetate, propionate, and butyrate, which
are metabolites fermented by gut microbiota, on the growth
of Enterococci. Enterococci were cultured in the presence
or absence of acetate, propionate, or butyrate, and the optical
density at 600 nm was measured to determine bacterial
growth. The minimum inhibitory concentration/minimum
bactericidal concentration test was conducted. Bacteria were
treated with a SCFA, together with clinically used endodontic
treatment methods such as triple antibiotics (metronidazole,
minocycline, and ciprofloxacin) and chlorhexidine gluconate
(CHX) to determine the effects of combination treatment.
Of the SCFAs, propionate had a bacteriostatic effect, inhibiting
the growth of E. faecalis in a dose-dependent manner and
also that of clinical strains of E. faecalis isolated from dental
plaques. Meanwhile, acetate and butyrate had minimal effects
on E. faecalis growth. Moreover, propionate inhibited the
growth of other Enterococci including E. faecium. In addition,
combination treatment of propionate and triple antibiotics
led to further growth inhibition, whereas no cooperative
effect was observed at propionate plus CHX. These results
indicate that propionate attenuates the growth of Enterococci,
suggesting propionate as a potential agent to control
Enterococcal infections, especially when combined with triple
antibiotics.
- Isolation, cultivation, and genome analysis of proteorhodopsincontaining SAR116-clade strain Candidatus Puniceispirillum marinum IMCC1322
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Junhak Lee , Kae Kyoung Kwon , Seung-Il Lim , Jaeho Song , Ah Reum Choi , Sung-Hyun Yang , Kwang-Hwan Jung , Jung-Hyun Lee , Sung Gyun Kang , Hyun-Myung Oh , Jang-Cheon Cho
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J. Microbiol. 2019;57(8):676-687. Published online June 14, 2019
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DOI: https://doi.org/10.1007/s12275-019-9001-2
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Abstract
- Strain IMCC1322 was isolated from a surface water sample
from the East Sea of Korea. Based on 16S rRNA analysis,
IMCC1322 was found to belong to the OCS28 sub-clade of
SAR116. The cells appeared as short vibrioids in logarithmicphase
culture, and elongated spirals during incubation with
mitomycin or in aged culture. Growth characteristics of strain
IMCC1322 were further evaluated based on genomic information;
proteorhodopsin (PR), carbon monoxide dehydrogenase,
and dimethylsulfoniopropionate (DMSP)-utilizing
enzymes. IMCC1322 PR was characterized as a functional
retinylidene protein that acts as a light-driven proton pump
in the cytoplasmic membrane. However, the PR-dependent
phototrophic potential of strain IMCC1322 was only observed
under CO-inhibited and nutrient-limited culture conditions.
A DMSP-enhanced growth response was observed in addition
to cultures grown on C1 compounds like methanol, formate,
and methane sulfonate. Strain IMCC1322 cultivation
analysis revealed biogeochemical processes characteristic of
the SAR116 group, a dominant member of the microbial community
in euphotic regions of the ocean. The polyphasic taxonomy
of strain IMCC1322 is given as Candidatus Puniceispirillum
marinum, and was confirmed by chemotaxonomic
tests, in addition to 16S rRNA phylogeny and cultivation
analyses.
Research Support, Non-U.S. Gov'ts
- Crystal structure and modeling of the tetrahedral intermediate state of methylmalonate-semialdehyde dehydrogenase (MMSDH) from Oceanimonas doudoroffii
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Hackwon Do , Chang Woo Lee , Sung Gu Lee , Hara Kang , Chul Min Park , Hak Jun Kim , Hyun Park , HaJeung Park , Jun Hyuck Lee
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J. Microbiol. 2016;54(2):114-121. Published online February 2, 2016
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DOI: https://doi.org/10.1007/s12275-016-5549-2
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Abstract
- The gene product of dddC (Uniprot code G5CZI2), from
the Gram-negative marine bacterium Oceanimonas doudoroffii,
is a methylmalonate-semialdehyde dehydrogenase
(OdoMMSDH) enzyme. MMSDH is a member of the aldehyde
dehydrogenase superfamily, and it catalyzes the NADdependent
decarboxylation of methylmalonate semialdehyde
to propionyl-CoA. We determined the crystal structure
of OdoMMSDH at 2.9 Å resolution. Among the twelve molecules
in the asymmetric unit, six subunits complexed with
NAD, which was carried along the protein purification steps.
OdoMMSDH exists as a stable homodimer in solution; each
subunit consists of three distinct domains: an NAD-binding
domain, a catalytic domain, and an oligomerization domain.
Computational modeling studies of the OdoMMSDH structure
revealed key residues important for substrate recognition
and tetrahedral intermediate stabilization. Two basic residues
(Arg103 and Arg279) and six hydrophobic residues (Phe150,
Met153, Val154, Trp157, Met281, and Phe449) were found to
be important for tetrahedral intermediate binding. Modeling
data also suggested that the backbone amide of Cys280 and
the side chain amine of Asn149 function as the oxyanion
hole during the enzymatic reaction. Our results provide useful insights into the substrate recognition site residues and
catalytic mechanism of OdoMMSDH.
- NOTE] Biosynthetic Pathway for Poly(3-Hydroxypropionate) in Recombinant Escherichia coli
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Qi Wang , Changshui Liu , Mo Xian , Yongguang Zhang , Guang Zhao
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J. Microbiol. 2012;50(4):693-697. Published online August 25, 2012
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DOI: https://doi.org/10.1007/s12275-012-2234-y
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Abstract
- Poly(3-hydroxypropionate) (P3HP) is a biodegradable and biocompatible thermoplastic. In this study, we engineered a P3HP biosynthetic pathway in recombinant Escherichia coli. The genes for malonyl-CoA reductase (mcr, from Chloroflexus aurantiacus), propionyl-CoA synthetase (prpE, from E. coli), and polyhydroxyalkanoate synthase (phaC1, from Ralstonia eutropha) were cloned and expressed in E. coli. The E. coli genes accABCD encoding acetyl-CoA carboxylase were used to channel the carbon into the P3HP pathway. Using glucose as a sole carbon source, the cell yield and P3HP content were 1.32 g/L and 0.98% (wt/wt [cell dry weight]), respectively. Although the yield is relatively low, our study shows the feasibility of engineering a P3HP biosynthetic pathway using a structurally unrelated carbon source in bacteria.
Published Erratum