Journal of Microbiology

Hana Im

3 Articles

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

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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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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

Rescue of a Cold-Sensitive Mutant at Low Temperatures by Cold Shock Proteins from Polaribacter irgensii KOPRI 22228: Ji-hyun Uh , Youn Hong Jung , Yoo Kyung Lee , Hong Kum Lee , Hana Im; J. Microbiol. 2010;48(6):798-802. Published online January 9, 2011; DOI: https://doi.org/10.1007/s12275-010-0402-5

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Abstract PDF

Exposure to low temperatures induces the biosynthesis of specific sets of proteins, including cold shock proteins (Csps). Since many of the specific functions of pychrophilic Csps are unknown, the roles of Csps from an Arctic bacterium, Polaribacter irgensii KOPRI 22228, were examined. The genes encoding CspA and CspC of P. irgensii were cloned in this study. Sequence analysis showed that these proteins have cold shock domains containing two RNA-binding motifs, RNP1 and RNP2. Both proteins bound oligo(dT)-cellulose resins, suggesting single-stranded nucleic acid-binding activity. When the P. irgensii Csps were overexpressed in Escherichia coli, the cold-resistance of the host was increased by more than five-fold. The P. irgensii Csps also rescued a cold-sensitive E. coli csp-quadruple deletion strain, BX04, at low temperatures. These results suggest that Csps from P. irgensii play a role in survival in polar environments.

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Cold Shock Protein B as an Alternative to DMSO for Oocyte Vitrification
Xinhai Wang, Jing Guo, Kaiyan Zhang, Yi Fang, Hongyu Liu, He Ding, Yang Lyu, Xin Ma, Wenfa Lyu
Antioxidants.2026; 15(1): 107. CrossRef
Metabolic Pathway of Phenol Degradation of a Cold-Adapted Antarctic Bacteria, Arthrobacter sp.
Gillian Li Yin Lee, Nur Nadhirah Zakaria, Hiroyuki Futamata, Kenshi Suzuki, Azham Zulkharnain, Noor Azmi Shaharuddin, Peter Convey, Khadijah Nabilah Mohd Zahri, Siti Aqlima Ahmad
Catalysts.2022; 12(11): 1422. CrossRef
CspB of an arctic bacterium, Polaribacter irgensii KOPRI 22228, confers extraordinary freeze-tolerance
Youn Hong Jung, Yoo Kyung Lee, Hong Kum Lee, Kyunghee Lee, Hana Im
Brazilian Journal of Microbiology.2018; 49(1): 97. CrossRef
Psychrophilic Enzymes: From Folding to Function and Biotechnology
Georges Feller
Scientifica.2013; 2013: 1. CrossRef

A Recombinant Human [alpha]_1-Antitrypsin Variant, M_malton, Undergoes a Spontaneous Conformational Conversion into a Latent Form: Chan-Hun Jung , Hana Im; J. Microbiol. 2003;41(4):335-339.

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Abstract PDF: Many genetic variants of [alpha]_1-antitrypsin have been associated with early onset emphysema and liver cirrhosis. However, the detailed structural basis of pathogenic [alpha]_1-antitrypsin molecules is rarely known. Here we found that a recombinant M_malton variant (Phe52-deleted) lost inhibitory activity by spontaneous conformational conversion into a more stable, inactive form under physiological conditions. Biochemical and spectroscopic data suggested that the variant converts into a reactive center loop-inserted conformation, resembling the latent form of plasminogen activator inhibitor-1.

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