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Kyungyun Cho 3 Articles
Tubulysins are Essential for the Preying of Ciliates by Myxobacteria
Uisang Yu , Jiha Kim , Seohui Park , Kyungyun Cho
J. Microbiol. 2023;61(6):627-632.   Published online June 14, 2023
DOI: https://doi.org/10.1007/s12275-023-00056-2
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  • 4 Web of Science
  • 3 Crossref
AbstractAbstract PDF
Tubulysins are bioactive secondary metabolites produced by myxobacteria that promote microtubule disassembly. Microtubules are required for protozoa such as Tetrahymena to form cilia and flagella. To study the role of tubulysins in myxobacteria, we co-cultured myxobacteria and Tetrahymena. When 4000 Tetrahymena thermophila and 5.0 × 108 myxobacteria were added to 1 ml of CYSE medium and co-cultured for 48 h, the population of T. thermophila increased to more than 75,000. However, co-culturing tubulysin-producing myxobacteria, including Archangium gephyra KYC5002, with T. thermophila caused the population of T. thermophila to decrease from 4000 to less than 83 within 48 h. Almost no dead bodies of T. thermophila were observed in the culture medium. Co-culturing of T. thermophila and the A. gephyra KYC5002 strain with inactivation of the tubulysin biosynthesis gene led to the population of T. thermophila increasing to 46,667. These results show that in nature, most myxobacteria are preyed upon by T. thermophila, but some myxobacteria prey on and kill T. thermophila using tubulysins. Adding purified tubulysin A to T. thermophila changed the cell shape from ovoid to spherical and caused cell surface cilia to disappear.

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Citations to this article as recorded by  
  • Analysis of gill and skin microbiota in Larimichthys crocea reveals bacteria associated with cryptocaryoniasis resistance potential
    Xiao Xie, Kangshuai Sun, Aowei Liu, Rujiang Miao, Fei Yin
    Fish & Shellfish Immunology.2025; 161: 110228.     CrossRef
  • Tubulysin Production by the Dead Cells of Archangium gephyra KYC5002
    Seohui Park, Chaehyeon Park, Yujin Ka, Kyungyun Cho
    Journal of Microbiology.2024; 62(6): 463.     CrossRef
  • Two reasons to kill: predation and kin discrimination in myxobacteria
    Christine Kaimer, Michael L. Weltzer, Daniel Wall
    Microbiology .2023;[Epub]     CrossRef
Mutants defective in the production of encapsulin show a tan-phaselocked phenotype in Myxococcus xanthus
Dohee Kim , Juo Choi , Sunjin Lee , Hyesook Hyun , Kyoung Lee , Kyungyun Cho
J. Microbiol. 2019;57(9):795-802.   Published online June 11, 2019
DOI: https://doi.org/10.1007/s12275-019-8683-9
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  • 13 Web of Science
  • 10 Crossref
AbstractAbstract PDF
Myxococcus xanthus, a myxobacterium, displays phase variation between yellow phase and tan phase. We found that deletion of the encA gene encoding encapsulin and the encF gene encoding a metalloprotease causes formation of tan colonies that never transform into yellow colonies. The encA and encF mutants were defective in the production of DKxanthene and myxovirescin. They did not produce extracellular polysaccharides; hence, the cells did not aggregate in liquid and showed reduced swarming on agar plates. The mutants had defective sporulation, but were rescued extracellularly by wild type cells. All these traits indicate that the encA and encF mutants are likely to be tan-phase-locked, and encapsulin has a close relationship with phase variation in M. xanthus. The encA and encF genes are localized in the same gene cluster, encBAEFG (MXAN_3557~MXAN_3553). Unlike the encA and encF genes, deletion of other genes in the cluster did not show tan-phase-locked phenotype.

Citations

Citations to this article as recorded by  
  • Encapsulated Ferritin-like Proteins: A Structural Perspective
    Elif Eren, Norman R. Watts, Felipe Montecinos, Paul T. Wingfield
    Biomolecules.2024; 14(6): 624.     CrossRef
  • A widespread bacterial protein compartment sequesters and stores elemental sulfur
    Robert Benisch, Michael P. Andreas, Tobias W. Giessen
    Science Advances.2024;[Epub]     CrossRef
  • Structure and heterogeneity of a highly cargo-loaded encapsulin shell
    Seokmu Kwon, Michael P. Andreas, Tobias W. Giessen
    Journal of Structural Biology.2023; 215(4): 108022.     CrossRef
  • Bacterial Nanocompartments: Structures, Functions, and Applications
    Harry Benjamin McDowell, Egbert Hoiczyk, Michael Y. Galperin
    Journal of Bacteriology.2022;[Epub]     CrossRef
  • Condensation and Protection of DNA by the Myxococcus xanthus Encapsulin: A Novel Function
    Ana V. Almeida, Ana J. Carvalho, Tomás Calmeiro, Nykola C. Jones, Søren V. Hoffmann, Elvira Fortunato, Alice S. Pereira, Pedro Tavares
    International Journal of Molecular Sciences.2022; 23(14): 7829.     CrossRef
  • Encapsulins
    Tobias W. Giessen
    Annual Review of Biochemistry.2022; 91(1): 353.     CrossRef
  • Advances in encapsulin nanocompartment biology and engineering
    Jesse A. Jones, Tobias W. Giessen
    Biotechnology and Bioengineering.2021; 118(1): 491.     CrossRef
  • Encapsulin nanocages: Protein encapsulation and iron sequestration
    Ana V. Almeida, Ana J. Carvalho, Alice S. Pereira
    Coordination Chemistry Reviews.2021; 448: 214188.     CrossRef
  • Discovery and characterization of a novel family of prokaryotic nanocompartments involved in sulfur metabolism
    Robert J Nichols, Benjamin LaFrance, Naiya R Phillips, Devon R Radford, Luke M Oltrogge, Luis E Valentin-Alvarado, Amanda J Bischoff, Eva Nogales, David F Savage
    eLife.2021;[Epub]     CrossRef
  • Nanotechnological Applications Based on Bacterial Encapsulins
    Javier M. Rodríguez, Carolina Allende-Ballestero, Jeroen J. L. M. Cornelissen, José R. Castón
    Nanomaterials.2021; 11(6): 1467.     CrossRef
Effect of gacS and gacA Mutations on Colony Architecture, Surface Motility, Biofilm Formation and Chemical Toxicity in Pseudomonas sp. KL28
Kyung Soon Choi , Yaligara Veeraragouda , Kyoung Mi Cho , Soo O Lee , Geuk Rae Jo , Kyungyun Cho , Kyoung Lee
J. Microbiol. 2007;45(6):492-498.
DOI: https://doi.org/2646 [pii]
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AbstractAbstract PDF
GacS and GacA proteins form a two component signal transduction system in bacteria. Here, Tn5 transposon gacS and gacA (Gac) mutants of Pseudomonas sp. KL28, an alkylphenol degrader, were isolated by selecting for smooth colonies of strain KL28. The mutants exhibited reduced ability to migrate on a solid surface. This surface motility does not require the action of flagella unlike the well-studied swarming motility of other Pseudomonas sp. The Gac mutants also showed reduced levels of biofilm and pellicle formation in liquid culture. In addition, compared to the wild type KL28 strain, these mutants were more resistant to high concentrations of m-cresol but were more sensitive to H2O2, which are characteristics that they share with an rpoS mutant. These results indicate that the Gac regulatory cascade in strain KL28 positively controls wrinkling morphology, biofilm formation, surface translocation and H2O2 resistance, which are important traits for its capacity to survive in particular niches.
Kyungyun Cho 1 Article
Tubulysin Production by the Dead Cells of Archangium gephyra KYC5002
Seohui Park, Chaehyeon Park, Yujin Ka, Kyungyun Cho
J. Microbiol. 2024;62(6):463-471.   Published online June 13, 2024
DOI: https://doi.org/10.1007/s12275-024-00130-3
  • 266 View
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  • 1 Scopus
AbstractAbstract PDF
Archangium gephyra KYC5002 produces tubulysins during the death phase. In this study, we aimed to determine whether dead cells produce tubulysins. Cells were cultured for three days until the verge of the death phase, disrupted via ultrasonication, incubated for 2 h, and examined for tubulysin production. Non-disrupted cells produced 0.14 mg/L of tubulysin A and 0.11 mg/L of tubulysin B. Notably, tubulysin A production was increased by 4.4-fold to 0.62 mg/L and that of tubulysin B was increased by 6.7-fold to 0.74 mg/L in the disrupted cells. The same increase in tubulysin production was observed when the cells were killed by adding hydrogen peroxide. However, when the enzymes were inactivated via heat treatment of the cultures at 65 °C for 30 min, no significant increase in tubulysin production due to cell death was observed. Reverse transcription-quantitative polymerase chain reaction analysis of tubB mRNA revealed that the expression levels of tubulysin biosynthetic enzyme genes increased during the death phase compared to those during the vegetative growth phase. Our findings suggest that A. gephyra produces biosynthetic enzymes and subsequently uses them for tubulysin production in the cell death phase or during cell lysis by predators.

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