Review
- 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
-
-
60
View
-
0
Download
-
1
Web of Science
-
2
Crossref
-
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.
-
Citations
Citations to this article as recorded by

- Host Immune Pathways to Mycobacterium tuberculosis Infection
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
Journal Article
- Isolation, cultivation, and genome analysis of proteorhodopsincontaining SAR116-clade strain Candidatus Puniceispirillum marinum IMCC1322
-
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
-
J. Microbiol. 2019;57(8):676-687. Published online June 14, 2019
-
DOI: https://doi.org/10.1007/s12275-019-9001-2
-
-
51
View
-
0
Download
-
12
Web of Science
-
11
Crossref
-
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.
-
Citations
Citations to this article as recorded by

- Effects of Light and Dark Conditions on the Transcriptome of Aging Cultures of Candidatus Puniceispirillum marinum IMCC1322
Ji Hyen Lee, Hyun-Myung Oh
Journal of Microbiology.2024; 62(4): 297. CrossRef - Identification of Structural and Morphogenesis Genes of Sulfitobacter Phage ΦGT1 and Placement within the Evolutionary History of the Podoviruses
Stephen C. Hardies, Byung Cheol Cho, Gwang Il Jang, Zhiqing Wang, Chung Yeon Hwang
Viruses.2023; 15(7): 1475. CrossRef - Seasonal niche differentiation among closely related marine bacteria
Adrià Auladell, Albert Barberán, Ramiro Logares, Esther Garcés, Josep M Gasol, Isabel Ferrera
The ISME Journal.2022; 16(1): 178. CrossRef - Cultivation of Dominant Freshwater Bacterioplankton Lineages Using a High-Throughput Dilution-to-Extinction Culturing Approach Over a 1-Year Period
Suhyun Kim, Md. Rashedul Islam, Ilnam Kang, Jang-Cheon Cho
Frontiers in Microbiology.2021;[Epub] CrossRef - Towards culturing the microbe of your choice
J. Cameron Thrash
Environmental Microbiology Reports.2021; 13(1): 36. CrossRef - Seasonal and annual changes in the microbial communities of Ofunato Bay, Japan, based on metagenomics
Atsushi Kobiyama, Jonaira Rashid, Md. Shaheed Reza, Yuri Ikeda, Yuichiro Yamada, Toshiaki Kudo, Nanami Mizusawa, Saki Yanagisawa, Daisuke Ikeda, Shigeru Sato, Takehiko Ogata, Kazuho Ikeo, Shinnosuke Kaga, Shiho Watanabe, Kimiaki Naiki, Yoshimasa Kaga, Sat
Scientific Reports.2021;[Epub] CrossRef - Aequoribacter fuscus gen. nov., sp. nov., a new member of the family Halieaceae, isolated from coastal seawater
Shan-Hui Li, Jaeho Song, Ilnam Kang, Juchan Hwang, Jang-Cheon Cho
Journal of Microbiology.2020; 58(6): 463. CrossRef - Functional Seasonality of Free-Living and Particle-Associated Prokaryotic Communities in the Coastal Adriatic Sea
Paul A. Steiner, Javier Geijo, Eduard Fadeev, Aleix Obiol, Eva Sintes, Thomas Rattei, Gerhard J. Herndl
Frontiers in Microbiology.2020;[Epub] CrossRef - High-throughput cultivation based on dilution-to-extinction with catalase supplementation and a case study of cultivating acI bacteria from Lake Soyang
Suhyun Kim, Miri S. Park, Jaeho Song, Ilnam Kang, Jang-Cheon Cho
Journal of Microbiology.2020; 58(11): 893. CrossRef - Advantages outweigh concerns about using genome sequence as type material for prokaryotic taxonomy
Konstantinos T. Konstantinidis, Ramon Rosselló‐Móra, Rudolf Amann
Environmental Microbiology.2020; 22(3): 819. CrossRef - Expanding the Diversity of Bacterioplankton Isolates and Modeling Isolation Efficacy with Large-Scale Dilution-to-Extinction Cultivation
Michael W. Henson, V. Celeste Lanclos, David M. Pitre, Jessica Lee Weckhorst, Anna M. Lucchesi, Chuankai Cheng, Ben Temperton, J. Cameron Thrash, Robert M. Kelly
Applied and Environmental Microbiology.2020;[Epub] CrossRef
Research Support, Non-U.S. Gov't
- Crystal structure and modeling of the tetrahedral intermediate state of methylmalonate-semialdehyde dehydrogenase (MMSDH) from Oceanimonas doudoroffii
-
Hackwon Do , Chang Woo Lee , Sung Gu Lee , Hara Kang , Chul Min Park , Hak Jun Kim , Hyun Park , HaJeung Park , Jun Hyuck Lee
-
J. Microbiol. 2016;54(2):114-121. Published online February 2, 2016
-
DOI: https://doi.org/10.1007/s12275-016-5549-2
-
-
43
View
-
0
Download
-
6
Crossref
-
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.
-
Citations
Citations to this article as recorded by

- Where do the electrons go? How numerous redox processes drive phytochemical diversity
Patrick J. Horn
Phytochemistry Reviews.2021; 20(2): 367. CrossRef - Crystal Structure of Aldehyde Dehydrogenase 16 Reveals Trans-Hierarchical Structural Similarity and a New Dimer
Li-Kai Liu, John J. Tanner
Journal of Molecular Biology.2019; 431(3): 524. CrossRef - Reconstructing the Electron Density of Intermediates of the Hydrolysis of N-Acetylaspartate by Aspartoacylase
M. G. Khrenova, E. D. Kots, A. M. Kulakova, A. V. Nemukhin
Russian Journal of Physical Chemistry A.2019; 93(10): 1873. CrossRef - NAD+ promotes assembly of the active tetramer of aldehyde dehydrogenase 7A1
David A. Korasick, Tommi A. White, Srinivas Chakravarthy, John J. Tanner
FEBS Letters.2018; 592(19): 3229. CrossRef - Expression and Interaction Analysis among Saffron ALDHs and Crocetin Dialdehyde
Lourdes Gómez-Gómez, Luis F. Pacios, Araceli Diaz-Perales, María Garrido-Arandia, Javier Argandoña, Ángela Rubio-Moraga, Oussama Ahrazem
International Journal of Molecular Sciences.2018; 19(5): 1409. CrossRef - X-ray crystal structure of a malonate-semialdehyde dehydrogenase fromPseudomonassp. strain AAC
Matthew Wilding, Colin Scott, Thomas S. Peat, Janet Newman
Acta Crystallographica Section F Structural Biology Communications.2017; 73(1): 24. CrossRef