Journal of Microbiology

Journal Articles

The inner membrane protein LapB is required for adaptation to cold stress in an LpxC-independent manner: Han Byeol Lee , Si Hyoung Park , Chang-Ro Lee; J. Microbiol. 2021;59(7):666-674. Published online May 15, 2021; DOI: https://doi.org/10.1007/s12275-021-1130-8

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The inner membrane protein lipopolysaccharide assembly protein B (LapB) is an adaptor protein that activates the proteolysis of LpxC by an essential inner membrane metalloprotease, FtsH, leading to a decrease in the level of lipopolysaccharide in the membrane. In this study, we revealed the mechanism by which the essential inner membrane protein YejM regulates LapB and analyzed the role of the transmembrane domain of LapB in Escherichia coli. The transmembrane domain of YejM genetically and physically interacted with LapB and inhibited its function, which led to the accumulation of LpxC. The transmembrane domain of LapB was indispensable for both its physical interaction with YejM and its regulation of LpxC proteolysis. Notably, we found that the lapB mutant exhibited strong cold sensitivity and this phenotype was not associated with increased accumulation of LpxC. The transmembrane domain of LapB was also required for its role in adaptation to cold stress. Taken together, these
results
showed that LapB plays an important role in both the regulation of LpxC level, which is controlled by its interaction with the transmembrane domain of YejM, and adaptation to cold stress, which is independent of LpxC.

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PhoPQ-mediated lipopolysaccharide modification governs intrinsic resistance to tetracycline and glycylcycline antibiotics in Escherichia coli
Byoung Jun Choi, Umji Choi, Dae-Beom Ryu, Chang-Ro Lee, Mehrad Hamidian, You-Hee Cho
mSystems.2024;[Epub] CrossRef
Lytic transglycosylase repertoire diversity enables intrinsic antibiotic resistance and daughter cell separation in Escherichia coli under acidic stress
Ji Eun Son, Si Hyoung Park, Umji Choi, Chang-Ro Lee, Laurent Poirel
Antimicrobial Agents and Chemotherapy.2024;[Epub] CrossRef
Trans-cinnamaldehyde inhibits Escherichia coli growth by regulating lipopolysaccharide accumulation
Huanling Xing, Xiaomin Liu, Jianhao Lin, Mingfei Sun, Junyi Huang, Xinghai Li, Yanqun Li, Shining Guo, Fang Zhou, Hong Wu
Food Bioscience.2024; 61: 104559. CrossRef
Coordinated and Distinct Roles of Peptidoglycan Carboxypeptidases DacC and DacA in Cell Growth and Shape Maintenance under Stress Conditions
Umji Choi, Si Hyoung Park, Han Byeol Lee, Ji Eun Son, Chang-Ro Lee, Cristina Solano
Microbiology Spectrum.2023;[Epub] CrossRef
NoiD, a DedA membrane protein required for homeostasis maintaining of Rhizobium leguminosarum biovar viciae during symbiosis with Pisum sativum
Xiaofang Li, Jiaming Xu, Yajuan Wei, Zirui Chen
Symbiosis.2022; 86(1): 81. CrossRef
Conserved Tandem Arginines for PbgA/YejM Allow Salmonella Typhimurium To Regulate LpxC and Control Lipopolysaccharide Biogenesis during Infection
Nicole P. Giordano, Joshua A. Mettlach, Zachary D. Dalebroux, Manuela Raffatellu
Infection and Immunity.2022;[Epub] CrossRef
Divergent Effects of Peptidoglycan Carboxypeptidase DacA on Intrinsic β-Lactam and Vancomycin Resistance
Si Hyoung Park, Umji Choi, Su-Hyun Ryu, Han Byeol Lee, Jin-Won Lee, Chang-Ro Lee, Krisztina M. Papp-Wallace
Microbiology Spectrum.2022;[Epub] CrossRef
Cryo-EM structure of transmembrane AAA+ protease FtsH in the ADP state
Wu Liu, Martien Schoonen, Tong Wang, Sean McSweeney, Qun Liu
Communications Biology.2022;[Epub] CrossRef
Checkpoints That Regulate Balanced Biosynthesis of Lipopolysaccharide and Its Essentiality in Escherichia coli
Gracjana Klein, Alicja Wieczorek, Martyna Szuster, Satish Raina
International Journal of Molecular Sciences.2021; 23(1): 189. CrossRef

Autophagic elimination of Trypanosoma cruzi in the presence of metals: Laís Pessanha de Carvalho , Edésio José Tenório de Melo; J. Microbiol. 2019;57(10):918-926. Published online August 28, 2019; DOI: https://doi.org/10.1007/s12275-019-9018-6

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Abstract

Trypanosoma cruzi is an obligate intracellular parasite transmitted to vertebrate hosts by blood-sucking insects. Molecules present in parasites and mammalian cells allow the recognition and parasite internalization. Metallic ions play an essential role in the establishment and maintenance of hostparasite interaction. However, little is known about how parasites handle with essential and nonessential metal quotas. This study aimed to investigate the influence of metal ions on the biological processes of T. cruzi infected cells. Infected cells were incubated with ZnCl2, CdCl2, and HgCl2 for 12 h and labeled with different specific dyes to investigate the cellular events related to intracellular parasite death and elimination. Infected host cells and parasite’s mitochondria underwent functional and structural disorders, in addition to parasite’s DNA condensation and pH decrease on host cells, which led to parasite death. Further investigations suggested that lysosomes were involved in pH decrease and the double membrane of the endoplasmic reticulum formed vacuoles surrounding damaged parasites, which indicate the occurrence of autophagy for parasite elimination. In conclusion, low concentrations of nonessential and essential metals cause a series of damage to Trypanosoma cruzi organelles, leading to its loss of viability, death, and elimination, with no removal of the host cells.

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The role of host autophagy in intracellular protozoan parasites diseases
Rafael Cardoso Maciel Costa Silva, Jhones Sousa Ribeiro, Thalita Santos de Moraes de Farias, Leonardo Holanda Travassos
Archives of Biochemistry and Biophysics.2024; 761: 110186. CrossRef
Personalized Prevention in Mercury-Induced Amyotrophic Lateral Sclerosis: A Case Report
Nicola Magnavita, Mario Sabatelli, Egeria Scoditti, Francesco Chirico
Applied Sciences.2020; 10(21): 7839. CrossRef
Essential and nonessential metal effects on extracellular Leishmania amazonensis in vitro
Laís Pessanha de Carvalho, Jana Held, Edésio José Tenório de Melo
Experimental Parasitology.2020; 209: 107826. CrossRef

Research Support, Non-U.S. Gov't

NOTE] A Protective Role of Methionine-R-Sulfoxide Reductase against Cadmium in Schizosaccharomyces pombe: Chang-Jin Lim , Hannah Jo , Kyunghoon Kim; J. Microbiol. 2014;52(11):976-981. Published online May 30, 2014; DOI: https://doi.org/10.1007/s12275-014-3512-7

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Abstract

The Schizosaccharomyces pombe cells harboring the methionine- R-sulfoxide reductase (MsrB)-overexpressing recombinant plasmid pFMetSO exhibited better growth than vector control cells, when shifted into fresh medium containing cadmium chloride (abbreviated as Cd). Although both groups of cells contained enhanced reactive oxygen species (ROS) and nitric oxide (NO) levels in the presence of Cd, ROS and NO levels were significantly lower in the S. pombe cells harboring pFMetSO than in vector control cells. Conversely, the S. pombe cells harboring pFMetSO possessed higher total glutathione (GSH) levels and a greater reduced/oxidized GSH ratio than vector control cells under the same conditions.

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Pleurotus pulmonarius Strain: Arsenic(III)/Cadmium(II) Accumulation, Tolerance, and Simulation Application in Environmental Remediation
Yuhui Zhang, Xiaohong Chen, Ling Xie
International Journal of Environmental Research and Public Health.2023; 20(6): 5056. CrossRef
Impact of cadmium and nickel on ion homeostasis in the yeast Schizosaccharomyces pombe
Miroslava Pozgajova, Alica Navratilova, Julius Arvay, Hana Duranova, Anna Trakovicka
Journal of Environmental Science and Health, Part B.2020; 55(2): 166. CrossRef
A methionine-R-sulfoxide reductase, OsMSRB5, is required for rice defense against copper toxicity
Tengwei Xiao, Mengmeng Mi, Changyong Wang, Meng Qian, Yahua Chen, Luqing Zheng, Hongsheng Zhang, Zhubing Hu, Zhenguo Shen, Yan Xia
Environmental and Experimental Botany.2018; 153: 45. CrossRef
Identification and Characterization of a Novel Methionine Sulfoxide Reductase B Gene (AccMsrB) fromApis cerana cerana(Hymenoptera: Apidae)
Feng Liu, Zhihong Gong, Weixing Zhang, Ying Wang, Lanting Ma, Hongfang Wang, Xingqi Guo, Baohua Xu
Annals of the Entomological Society of America.2015; 108(4): 575. CrossRef

Effect of Zinc and Calcium on the Intracelularly uptake of Cadimium and growth of Escherichia coli: Hong, Hyo Bong , Brown, Lewis R. , Kim, Jong Kyu; J. Microbiol. 1995;33(4):302-306.

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Abstract: E. coli was tested for their ability to uptake cadmium intracellularly, and the effect of zinc and calcium on cadmium toxicity to E. coli was observed. In addition, the effect of zinc and calcium on the uptake of cadimium was also studied. This study showed that living E. coli cells took up more cadmium than the dead cells. E. coli in the log phase uptake cadimiumm more actively than E. coli in the stationary phase. These results suggested that there may be metabolic reactions or compounds which encourage the uptake of cadimium. This study also showed that cadimium was sequestered by cell components of which molecular weight is about 30,000. Adding of zinc and calcium chloride reduced cadmium toxicity in E. coli and encouraged intracellular uptake by E coli. However adding of heavy metal solutions helped the microorganisms to adsorb more cadmium. Extremely high or low concentrations of zinc, however, did not affect cell viability.

Characterization of azomonas agilis PY101, a cadmium-resistant strain isolated from anyang stream: You, Kyung Man , Lee, Ji Hyun , Kim, Jeong Kook , Hah, Nam Ju , Lee, Yung Nok , Park, Yong Keun; J. Microbiol. 1996;34(3):289-293.

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Abstract: A cadimium-resistant strain isolated from Anyang stream, Azomonas agilis PY101 exhibited strong resistance to 1000 ppm of cadmium ion (Cd^2+). A agilis PY101 also exhibited resistance to various antibiotics, such as amoxicillin, amplicilin, bacitracin, cefazolin, erythromycin, penicilin, tetracycline, and vancomycin. In the presence of Cd^2+, the growth of A. aglis PY101 started after an extended lag phase and produced a green-fluorescent pigment induced by cadmium. The dramatic decrease (approximately 400ppm) of concentration of cd^2+ in the culture medium during the growth phase of A. agilis PY101 was confirmed by the inductively coupled plasma-atomic emission spectrophotometer. Transmission electron microscopic analysis revealed that A. agilis PY 101 actively accumulated Cd^2+ in the cytoplasm.

Adaptaion of Azomonas agilis PY101 Exposed to Cadmium vua Production of Cadmium-Binding Pigment Promoted by Cd^2+: You, Kyung Man , Park, Yong Keun; J. Microbiol. 1998;36(3):159-163.

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Abstract: Azomonas agilis PY101 produced a fluorescent yellow-green pigment promoted by cadmium. The amount of extracellular pigment produced during the growth of A. agilis PY101 increased to approximately 6 times its initial value after the addition to 1.0 mg/ml of CdCl_2. The pigment peak(peak II) was observed when the supernatant solution acquired from the cells cultivated in the presence of cadmium was fractionated on a column of Superdex 75. Peak II contained about 70% of extracellular cadmium in the supernatant solution. This cadmium-binding pigment contained several sulfur-containing groups. The dramatic decrease (97%) of sulfate ion (SO_4^-2)concentration in the cytoplasm from 9.60 to 0.25 ㎍/ml during the growth of A. agilis PY101 under cadmium stress was confirmed by ion chromatography. Moreover, transmission electron microscopic analysis showed that Z. agilis PY101 actively accumulated cadmium in the interior of the cells. It appears that the cadmium adaptation of A. agilis PY101 is achieved by the microbial binding of the sulfur-containing pigment to cadmium.

Isolation and Characterization of Pigment-deficient Mutants from Azomonas agilis PY101: You, Kyung Man , Lee, Sang Hyeon , Park, Yong Keun; J. Microbiol. 1999;37(1):45-49.

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Abstract: To investigate the mechanism of cadmium tolerance in a cadmium-resistant Azomonas agilis PY101 that produces a specific fluorescent pigment promoted by cadmium, we carried out Tn5 mutagenesis and isolated four pigment-deficient mutants. In these mutants, Ppg1, Ppg2, and Ppg3 remarkably reduced the pigment production to 15.3%, 11.2%, and 13.9%, respectively. Especially, Ppg4 mutant did not produce the pigment at all. None of the mutants grew in the presence of 1500 ppm of CdCl₂in growth medium, and they exhibited differential sensitivities to cadmium. Ppg1, Ppg2, Ppg3, and Ppg4 mutants were sensitive to 900 ppm, 1100 ppm, 1000 ppm, and 800 ppm of CdCl2, respectively. These mutants also showed noticeable increase, from 8.8-fold to 13.2-fold, in the size of growth inhibition zone compared with that of the will type after treatment with cadmium. Therefore, the pigment production of A. agilis PY101 was found to decrease the toxic effects of cadmium to the bacterium.

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