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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
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AbstractAbstract
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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  • 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
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  • 12 Web of Science
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AbstractAbstract
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

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  • 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
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AbstractAbstract
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.

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  • 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

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