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- Pioneering strategies for overcoming bacterial drug resistance (2026)
- Advancing microbial engineering through synthetic biology (2025)
- Host-associated microbiome (2024)
- Bacterial regulatory mechanisms for the control of complex cellular mechanisms (2023)
- Two years into COVID-19 pandemic: Where are we? (2022)
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Article
- Impact of small RNA RaoN on nitrosative-oxidative stress resistance and virulence of Salmonella enterica serovar Typhimurium
- Sinyeon Kim , Yong Heon Lee
- J. Microbiol. 2020;58(6):499-506. Published online April 11, 2020
- DOI: https://doi.org/10.1007/s12275-020-0027-2
- 503 View
- 1 Download
- 6 Web of Science
- 7 Crossref
-
Abstract
PDF -
RaoN is a Salmonella-specific small RNA that is encoded in
the cspH-envE intergenic region on Salmonella pathogenicity
island-11. We previously reported that RaoN is induced under
conditions of acid and oxidative stress combined with nutrient
limitation, contributing to the intramacrophage growth
of Salmonella enterica serovar Typhimurium. However, the
role of RaoN in nitrosative stress response and virulence has
not yet been elucidated. Here we show that the raoN mutant
strain has increased susceptibility to nitrosative stress by
using a nitric oxide generating acidified nitrite. Extending
previous research on the role of RaoN in oxidative stress resistance,
we found that NADPH oxidase inhibition restores
the growth of the raoN mutant in LPS-treated J774A.1 macrophages.
Flow cytometry analysis further revealed that the
inactivation of raoN leads to an increase in the intracellular
level of reactive oxygen species (ROS) in Salmonella-infected
macrophages, suggesting that RaoN is involved in the inhibition
of NADPH oxidase-mediated ROS production by mechanisms
not yet resolved. Moreover, we evaluated the effect
of raoN mutation on the virulence in murine systemic
infection and determined that the raoN mutant is less virulent
than the wild-type strain following oral inoculation. In
conclusion
, small regulatory RNA RaoN controls nitrosativeoxidative stress resistance and is required for virulence of Salmonella in mice. -
Citations
Citations to this article as recorded by
- Site-2 protease-like protein drives organic solvent tolerance in Rhodococcus ruber
Jinfang Wu, Zhonghao Wu, Ren Peng
Journal of Microbiological Methods.2025; 236: 107204. CrossRef - The Salmonella enterica EnvE is an Outer Membrane Lipoprotein and Its Gene Expression Leads to Transcriptional Repression of the Virulence Gene msgA
Sinyeon Kim, Yong Heon Lee
Journal of Microbiology.2024; 62(11): 1013. CrossRef - Functions of Small Non-Coding RNAs in Salmonella–Host Interactions
Xia Meng, Mengping He, Pengpeng Xia, Jinqiu Wang, Heng Wang, Guoqiang Zhu
Biology.2022; 11(9): 1283. CrossRef - Detoxification Response of Pseudomonas fluorescens MFAF76a to Gaseous Pollutants NO2 and NO
Thibault Chautrand, Ségolène Depayras, Djouhar Souak, Mathilde Bouteiller, Tatiana Kondakova, Magalie Barreau, Mohamed Amine Ben Mlouka, Julie Hardouin, Yoan Konto-Ghiorghi, Sylvie Chevalier, Annabelle Merieau, Nicole Orange, Cécile Duclairoir-Poc
Microorganisms.2022; 10(8): 1576. CrossRef - Regulator of RNase E activity modulates the pathogenicity of Salmonella Typhimurium
Jaejin Lee, Eunkyoung Shin, Ji-Hyun Yeom, Jaeyoung Park, Sunwoo Kim, Minho Lee, Kangseok Lee
Microbial Pathogenesis.2022; 165: 105460. CrossRef - Gaseous NO2 induces various envelope alterations in Pseudomonas fluorescens MFAF76a
Thibault Chautrand, Ségolène Depayras, Djouhar Souak, Tatiana Kondakova, Magalie Barreau, Takfarinas Kentache, Julie Hardouin, Ali Tahrioui, Olivier Thoumire, Yoan Konto-Ghiorghi, Corinne Barbey, Guy Ladam, Sylvie Chevalier, Hermann J. Heipieper, Nicole O
Scientific Reports.2022;[Epub] CrossRef - Current challenges facing one-step production of l-ascorbic acid
Panpan Wang, Weizhu Zeng, Sha Xu, Guocheng Du, Jingwen Zhou, Jian Chen
Biotechnology Advances.2018; 36(7): 1882. CrossRef
- Site-2 protease-like protein drives organic solvent tolerance in Rhodococcus ruber
Research Support, Non-U.S. Gov't
- Identification of Chaperones in Freeze Tolerance in Saccharomyces cerevisiae
- Mahendran Chinnamara Naicker , I Seul Jo , Hana Im
- J. Microbiol. 2012;50(5):882-887. Published online November 4, 2012
- DOI: https://doi.org/10.1007/s12275-012-2411-z
- 283 View
- 0 Download
- 9 Crossref
-
Abstract
PDF
- Exposure to low temperatures reduces protein folding rates and induces the cold denaturation of proteins. Considering the roles played by chaperones in facilitating protein folding and preventing protein aggregation, chaperones must exist that confer tolerance to cold stress. Here, yeast strains lacking individual chaperones were screened for reduced freezing tolerance. In total, 19 of 82 chaperone-deleted strains tested were more sensitive to freeze-thaw treatment than wild-type cells. The reintroduction of the respective chaperone genes into the deletion mutants recovered the freeze tolerance. The freeze sensitivity of the chaperone-knockout strains was also retained in the presence of 20% glycerol.
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Citations
Citations to this article as recorded by- Systematic Characterization and Analysis of the Freeze–Thaw Tolerance Gene Set in the Budding Yeast, Saccharomyces cerevisiae
Donovan Hartnett, Michael Dotto, Ashley Aguirre, Sophia Brandao, Melanie Chauca, Sandra Chiang, Madison Cronin, Niti Deokar, Autum Martin, Zuri McCune, Joseph Onwusogh, Arisbeth Paulino-Cruz, Angelina D. Gonzalez Soto, Aisha Swaray, Maxwell Verdiner, Majd
International Journal of Molecular Sciences.2025; 26(5): 2149. CrossRef - Enhancing Freezing Stress Tolerance through Regulation of the Ubiquitin–Proteasome System in Saccharomyces cerevisiae
Ryoya Tanahashi, Akira Nishimura, Kyoyuki Kan, Natsumi Ishizaki, Shiho Fujishima, Hisanori Endo, Hiroshi Takagi
Fermentation.2024; 10(6): 318. CrossRef - Chaperone requirements for de novo folding of Saccharomyces cerevisiae septins
Daniel Hassell, Ashley Denney, Emily Singer, Aleyna Benson, Andrew Roth, Julia Ceglowski, Marc Steingesser, Michael McMurray, Amy Gladfelter
Molecular Biology of the Cell.2022;[Epub] CrossRef - Reinforcement of the Unfolded Protein Response Mitigates Cytotoxicity Induced by Human Z‐Type α1‐Antitrypsin
Jaeyeon Lim, Kyunghee Lee, Hana Im
Bulletin of the Korean Chemical Society.2021; 42(6): 900. CrossRef - Peptidyl‐Prolyl Isomerase Cpr7p of Yeast Prevents Protein Aggregation Upon Freezing
Seung Hyun Lee, Yang‐Hee Kim, Kyunghee Lee, Hana Im
Bulletin of the Korean Chemical Society.2018; 39(11): 1248. CrossRef - Micromanaging freeze tolerance: the biogenesis and regulation of neuroprotective microRNAs in frozen brains
Hanane Hadj-Moussa, Kenneth B. Storey
Cellular and Molecular Life Sciences.2018; 75(19): 3635. CrossRef - Molecular Physiology of Freeze Tolerance in Vertebrates
Kenneth B. Storey, Janet M. Storey
Physiological Reviews.2017; 97(2): 623. CrossRef - Yeast Cyclophilins Prevent Cold Denaturation of Proteins
Mahendran Chinnamara Naicker, Yang‐Hee Kim, Kyunghee Lee, Hana Im
Bulletin of the Korean Chemical Society.2016; 37(3): 366. CrossRef - Molecular Biology of Freezing Tolerance
Kenneth B. Storey, Janet M. Storey
Comprehensive Physiology.2013; 3(3): 1283. CrossRef
- Systematic Characterization and Analysis of the Freeze–Thaw Tolerance Gene Set in the Budding Yeast, Saccharomyces cerevisiae
Retracted Publication
- Identification of the Vibrio vulnificus htpG Gene and Its Influence on Cold Shock Recovery
- Slae Choi , Kyungku Jang , Seulah Choi , Hee-jee Yun , Dong-Hyun Kang
- J. Microbiol. 2012;50(4):707-711. Published online August 25, 2012
- DOI: https://doi.org/10.1007/s12275-012-2294-z
- 360 View
- 0 Download
- 7 Crossref
-
Abstract
PDF
- An htpG gene encoding the heat shock protein HtpG was identified and cloned from Vibrio vulnificus. The deduced amino acid sequence of HtpG from V. vulnificus exhibited 71 and 85% identity to those reported from Escherichia coli and V. cholera, respectively. Functions of HtpG were assessed by the construction of an isogenic mutant whose htpG gene was deleted and by evaluating its phenotype changes during and after cold shock. The results demonstrated that recovery of the wild type from cold shock was significantly faster (p<0.05) than that of the htpG mutant, and indicated that the chaperone protein HtpG contributes to cold shock recovery, rather than cold shock tolerance, of V. vulnificus.
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Citations
Citations to this article as recorded by- HtpG Is a Metal-Dependent Chaperone Which Assists the DnaK/DnaJ/GrpE Chaperone System of Mycobacterium tuberculosis via Direct Association with DnaJ2
Nikita Mangla, Ramandeep Singh, Nisheeth Agarwal, Gyanu Lamichhane
Microbiology Spectrum.2023;[Epub] CrossRef - Transcriptomic Adaptation of Legionella pneumophila to Transient Heat Shock
Jeffrey Liang, Sebastien P. Faucher
Frontiers in Water.2022;[Epub] CrossRef - The Bacterial Hsp90 Chaperone: Cellular Functions and Mechanism of Action
Sue Wickner, Thu-Lan Lily Nguyen, Olivier Genest
Annual Review of Microbiology.2021; 75(1): 719. CrossRef - Virulence of HtpG+ and HtpG− strains of Yersinia pestis for Mice and Guinea Pigs
E. A. Krasil’nikova, R. Z. Shaikhutdinova, T. E. Svetoch, M. E. Platonov, T. I. Kombarova, S. A. Ivanov, S. V. Dentovskaya, A. P. Anisimov
Problems of Particularly Dangerous Infections.2020; (2): 86. CrossRef - Proteomic profiling of integral membrane proteins associated to pathogenicity in Vibrio parahaemolyticus strains
Jesús A. Pérez‐Acosta, Marcel Martínez‐Porchas, José M. Elizalde‐Contreras, Juan Manuel Leyva, Eliel Ruiz‐May, Teresa Gollas‐Galván, Luis R. Martínez‐Córdova, José Ángel Huerta‐Ocampo
Microbiology and Immunology.2018; 62(1): 14. CrossRef - Stable isotope labelling by amino acids in cell culture (SILAC) applied to quantitative proteomics of Edwardsiella tarda ATCC 15947 under prolonged cold stress
Weixing Ma, Juntao Jia, Xiaohua Huang, Wancui Xie, Xiaoliang Zhang, Jing Tang, Chao Lin, Liqing Zhao, Peipei Fang
Microbial Pathogenesis.2018; 125: 12. CrossRef - High-Temperature Protein G Is an Essential Virulence Factor of Leptospira interrogans
Amy M. King, Gabriela Pretre, Thanatchaporn Bartpho, Rasana W. Sermswan, Claudia Toma, Toshihiko Suzuki, Azad Eshghi, Mathieu Picardeau, Ben Adler, Gerald L. Murray, S. R. Blanke
Infection and Immunity.2014; 82(3): 1123. CrossRef
- HtpG Is a Metal-Dependent Chaperone Which Assists the DnaK/DnaJ/GrpE Chaperone System of Mycobacterium tuberculosis via Direct Association with DnaJ2
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