Journal of Microbiology

Jinmi Kim

9 Articles

Apoptotic Factors, CaNma111 and CaYbh3, Function in Candida albicans Filamentation by Regulating the Hyphal Suppressors, Nrg1 and Tup1: Suyoung Kim , Se Hyeon Kim , Eunjoong Kweon , Jinmi Kim; J. Microbiol. 2023;61(4):403-409. Published online March 27, 2023; DOI: https://doi.org/10.1007/s12275-023-00034-8

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The morphological switch from the yeast to hyphal form is a key virulence attribute of the opportunistic fungal pathogen, Candida albicans. Our recent report showed that deletion of the newly identified apoptotic factor, CaNma111 or CaYbh3, leads to hyperfilamentation and increased virulence in a mouse infection model. CaNma111 and CaYbh3 are homologs of the pro-apoptotic protease, HtrA2/Omi, and BH3-only protein, respectively. In this study, we examined the effects of CaNMA111 and CaYBH3 deletion mutations on the expression levels of the hypha-specific transcr!ption factors, Cph1 (a hyphal activator), Nrg1 (a hyphal repressor), and Tup1 (a hyphal repressor). The protein levels of Nrg1 were decreased in Caybh3/Caybh3 cells while those of Tup1 were decreased in both Canma111/Canma111 and Caybh3/Caybh3 cells. These effects on Nrg1 and Tup1 proteins were retained during serum-induced filamentation and appear to explain the hyperfilamentation phenotypes of the CaNMA111 and CaYBH3 deletion mutants. Treatment with the apoptosis-inducing dose of farnesol decreased the Nrg1 protein levels in the wild-type strain and more evidently in Canma111/Canma111 and Caybh3/Caybh3 mutant strains. Together, our results suggest that CaNma111 and CaYbh3 are key regulators of Nrg1 and Tup1 protein levels in C. albicans.

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Candida albicans Extracellular Vesicles Upregulate Nrg1 Transcription Repressor to Inhibit Self-Hyphal Development and Candidemia
Yu Wei, Yujie Zhou, Bolei Li, Zheng Wang, Binyou Liao, Jiannan Wang, Jingzhi Zhou, Yawen Zong, Ding Chen, Jiawei Shen, Yangyang Shi, Xuedong Zhou, Ga Liao, Lichen Gou, Zhuoli Zhu, Lei Cheng, Biao Ren
International Journal of Molecular Sciences.2026; 27(1): 495. CrossRef
Moh1 coordinates ROS-dependent apoptosis in genotoxic stress response of Candida albicans
Jia Wang, Wenxia Gao, Xinyi Tang, Jinrong Feng
Fungal Biology.2025; 129(6): 101642. CrossRef

Fus3 and Tpk2 protein kinases regulate the phosphorylation-dependent functions of RNA helicase Dhh1 in yeast mating and Ste12 protein expression: Jaehee Hwang , Daehee Jung , Jinmi Kim; J. Microbiol. 2022;60(8):843-848. Published online July 14, 2022; DOI: https://doi.org/10.1007/s12275-022-2213-x

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Abstract PDF: Decapping of mRNA is a key regulatory step for mRNA decay and translation. The RNA helicase, Dhh1, is known as a decapping activator and translation repressor in yeast Saccharomyces cerevisiae. Dhh1 also functions as a gene-specific positive regulator in the expression of Ste12, a mating-specific transcription factor. A previous study showed that the Nerminal phosphorylation of Dhh1 regulates its association with the mRNA-binding protein, Puf6, to affect the protein translation of Ste12. Here, we investigated the roles of the phosphorylated residues of Dhh1 in yeast mating process and Ste12 expression. The phospho-deficient mutation, DHH1- T10A, was associated with decreased diploid formation during mating and decreased level of the Ste12 protein in response to α-mating pheromone. A kinase overexpression analysis revealed that Ste12 protein expression was affected by overexpression of Fus3 MAP kinase or Tpk2 kinase. Tpk2 was shown to be responsible for phosphorylation of Dhh1 at Thr10. Our study shows that overexpression of Fus3 or Tpk2 alters the Dhh1-Puf6 protein interaction and thereby affects Ste12 protein expression.

Roles of Dhh1 RNA helicase in yeast filamentous growth: Analysis of N-terminal phosphorylation residues and ATPase domains: Eunji Lee , Daehee Jung , Jinmi Kim; J. Microbiol. 2020;58(10):853-858. Published online September 29, 2020; DOI: https://doi.org/10.1007/s12275-020-0431-7

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In yeast Saccharomyces cerevisiae, the Dhh1 protein, a member of the DEAD-box RNA helicase, stimulates Dcp2/Dcp1- mediated mRNA decapping and functions as a general translation repressor. Dhh1 also positively regulates translation of a selected set of mRNAs, including Ste12, a transcription factor for yeast mating and pseudohyphal growth. Given the diverse functions of Dhh1, we investigated whether the putative phosphorylation sites or the conserved motifs for the DEADbox RNA helicases were crucial in the regulatory roles of Dhh1 during pseudohyphal growth. Mutations in the ATPase A or B motif (DHH1-K96R or DHH1-D195A) showed significant defects in pseudohyphal colony morphology and agar invasive phenotypes. The N-terminal phospho-mimetic mutation, DHH1-T16E, showed defects in pseudohyphal phenotypes. Decreased levels of Ste12 protein were also observed in these pseudohyphal-defective mutant cells under filamentous- inducing low nitrogen conditions. We suggest that the ATPase motifs and the Thr16 phosphorylation site of Dhh1 are crucial to its regulatory roles in pseudohyphal growth under low nitrogen conditions.

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Roles of P-body factors in Candida albicans filamentation and stress response
Melissa A. Tosiano, Frederick Lanni, Aaron P. Mitchell, C. Joel McManus, Guilhem Janbon
PLOS Genetics.2025; 21(3): e1011632. CrossRef
Biological implications of decapping: beyond bulk mRNA decay
Fivos Borbolis, Popi Syntichaki
The FEBS Journal.2022; 289(6): 1457. CrossRef
The Complex Genetic Basis and Multilayered Regulatory Control of Yeast Pseudohyphal Growth
Anuj Kumar
Annual Review of Genetics.2021; 55(1): 1. CrossRef

Roles of eIF4E-binding protein Caf20 in Ste12 translation and P-body formation in yeast: Kiyoung Park , Yu-Seon Lee , Daehee Jung , Jinmi Kim; J. Microbiol. 2018;56(10):744-747. Published online August 22, 2018; DOI: https://doi.org/10.1007/s12275-018-8230-0

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Translation initiation factor eIF4E forms eIF4E-eIF4G complex at the 5’ cap of mRNA. This interaction can be inhibited by the family of 4E-binding proteins (4E-BP). In yeast Saccharomyces cerevisiae, two 4E-BPs, Caf20 and Eap1, compete with eIF4G for binding to eIF4E via the shared conserved interaction motif. In order to investigate the roles of Caf20 in gene-specific translational regulation and the formation of mRNA granules (P-bodies), we introduced substitution mutations, caf20-Y4A or caf20-L9A, in the eIF4E-binding motif for CAF20. Overexpression of the wild-type CAF20 showed an increased protein level of Ste12 transcription factor as well as highly developed P-body formation. However, 4E-binding site mutations of CAF20 led to a reduced number of P-body foci and decreased levels of Ste12 protein. The phenotypes of the caf20 deletion mutation were also analyzed, and we suggest that Caf20 plays a critical role in Ste12 protein expression and in the control of P-body formation.

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Long Noncoding RNAs Responding to Ethanol Stress in Yeast Seem Associated with Protein Synthesis and Membrane Integrity
Amanda Piveta Schnepper, Agatha M. S. Kubo, Camila Moreira Pinto, Ramon Hernany Martins Gomes, Matheus Naia Fioretto, Luís Antonio Justulin, Aline M. M. Braz, Marjorie de Assis Golim, Rejane M. T. Grotto, Guilherme Targino Valente
Genes.2025; 16(2): 170. CrossRef
Proteomic analysis revealed the roles of YRR1 deletion in enhancing the vanillin resistance of Saccharomyces cerevisiae
Wenyan Cao, Weiquan Zhao, Bolun Yang, Xinning Wang, Yu Shen, Tiandi Wei, Wensheng Qin, Zailu Li, Xiaoming Bao
Microbial Cell Factories.2021;[Epub] CrossRef
Functional association of Loc1 and Puf6 with RNA helicase Dhh1 in translational regulation of Saccharomyces cerevisiae Ste12
Daehee Jung, Jong Seok Seo, Jayoung Nam, Jinmi Kim, Enrico Baruffini
PLOS ONE.2019; 14(7): e0220137. CrossRef

Mutational analysis of the RNA helicase Dhh1 in Ste12 expression and yeast mating: Daehee Jung , Jihye Ahn , Boram Rhee , Jinmi Kim; J. Microbiol. 2017;55(5):373-378. Published online April 29, 2017; DOI: https://doi.org/10.1007/s12275-017-7020-4

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Dhh1 and Dhh1 homologues (RCK/p54/DDX6) are mem-bers of the DEAD-box protein family of RNA helicases. These proteins display conserved sequence motifs for ATPase and RNA binding activities. Dhh1 is a component of the P-bodies (processing bodies) of mRNA granules and functions as an mRNA decapping activator in Saccharomyces cerevisiae. Dhh1 also contributes to gene-specific regulation during yeast mating. The dhh1 deletion mutation results in a significant decrease in the expression of Ste12, a mating-specific trans-cription factor, showing severe mating defects. Here, we in-troduced amino-acid substitution mutations in the ATPase and RNA binding domains of Dhh1 and also constructed a deletion of 79 amino acids at the Q/P-rich C-terminal region. The mutations in ATPase A and B motif (K96R, D195A) and C-terminus deletion showed reduced levels of mating effi-ciency as well as Ste12 protein expression. The Q/P-rich C- terminal region of Dhh1 was dispensable for growth at non- permissive temperature 37°C but appeared to play an im-portant role in regulating the Ste12 protein expression and mating processes. The P-body accumulation induced by treatment with α-mating factor required ATPase, RNA-bind-ing and the Q/P-rich C-terminal domains of Dhh1.

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Postharvest biocontrol ability and antagonistic mechanism of Streptomyces djakartensis MEPS155 against Ceratocystis fimbriata in sweetpotato
Yongjing Zhang, Xiaoying Cao, Changgen Li, Hao Cong, Yujie Chen, Qiao Liu, Yiming Wang, Hailan Fu, Jiluan Zhang, Jihong Jiang, Ludan Li
Postharvest Biology and Technology.2025; 229: 113709. CrossRef
Fus3 and Tpk2 protein kinases regulate the phosphorylation-dependent functions of RNA helicase Dhh1 in yeast mating and Ste12 protein expression
Jaehee Hwang, Daehee Jung, Jinmi Kim
Journal of Microbiology.2022; 60(8): 843. CrossRef
The Role of DEAD-Box ATPases in Gene Expression and the Regulation of RNA–Protein Condensates
Karsten Weis, Maria Hondele
Annual Review of Biochemistry.2022; 91(1): 197. CrossRef
Roles of Dhh1 RNA helicase in yeast filamentous growth: Analysis of N-terminal phosphorylation residues and ATPase domains
Eunji Lee, Daehee Jung, Jinmi Kim
Journal of Microbiology.2020; 58(10): 853. CrossRef
Functional association of Loc1 and Puf6 with RNA helicase Dhh1 in translational regulation of Saccharomyces cerevisiae Ste12
Daehee Jung, Jong Seok Seo, Jayoung Nam, Jinmi Kim, Enrico Baruffini
PLOS ONE.2019; 14(7): e0220137. CrossRef
Roles of eIF4E-binding protein Caf20 in Ste12 translation and P-body formation in yeast
Kiyoung Park, Yu-Seon Lee, Daehee Jung, Jinmi Kim
Journal of Microbiology.2018; 56(10): 744. CrossRef

Identification of Psk2, Skp1, and Tub4 as trans-acting factors for uORF-containing ROK1 mRNA in Saccharomyces cerevisiae: Soonmee Jeon , Suran Lim , Jeemin Ha , Jinmi Kim; J. Microbiol. 2015;53(9):616-622. Published online August 27, 2015; DOI: https://doi.org/10.1007/s12275-015-5389-5

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Rok1, a DEAD-box RNA helicase, is involved in rRNA processing and the control of cell cycle progression in Saccharomyces cerevisiae. Rok1 protein expression is cell cycle-regulated, declining at G1/S and increasing at G2. The downregulation of Rok1 expression in G1/S phase is mediated by the inhibitory action of two upstream open reading frames (uORFs) in the ROK1 5􍿁-untranslated region (5􍿁UTR). We identified Psk2 (PAS kinase), Skp1 (kinetochore protein) and Tub4 (γ-tubulin protein) as ROK1 5􍿁UTR-interacting proteins using yeast three-hybrid system. A deletion analysis of PSK2 or inactivation of temperature-sensitive alleles of SKP1 and TUB4 revealed that Rok1 protein synthesis is repressed by Psk2 and Skp1. This repression appeared to be mediated through the ROK1 uORF1. In contrast, Tub4 plays a positive role in regulating Rok1 protein synthesis and likely after the uORF1-mediated inhibitory regulation. These results suggest that 5􍿁UTR-interacting proteins, identified using three hybrid screening, are important for uORF-mediated regulation of Rok1 protein expression.

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Effects of rok1 gene deletion on mitosis in fission yeast at appropriate and stressful temperatures and the molecular mechanisms
Jiayi He, Mengnan Liu, Jiani Xu, Xiang Ding, Yiling Hou
Experimental and Therapeutic Medicine.2026; 31(6): 1. CrossRef
Identification of short open reading frames in plant genomes
Yong Feng, Mengyun Jiang, Weichang Yu, Jiannan Zhou
Frontiers in Plant Science.2023;[Epub] CrossRef
HST1 increases replicative lifespan of a sir2Δ mutant in the absence of PDE2 in Saccharomyces cerevisiae
Woo Kyu Kang, Mayur Devare, Jeong-Yoon Kim
Journal of Microbiology.2017; 55(2): 123. CrossRef

Deletion analysis of LSm, FDF, and YjeF domains of Candida albicans Edc3 in hyphal growth and oxidative-stress response: Eung-Chul Kim , Jinmi Kim; J. Microbiol. 2015;53(2):111-115. Published online January 28, 2015; DOI: https://doi.org/10.1007/s12275-015-4727-y

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Candida albicans is an opportunistic fungal pathogen whose responses to environmental changes are associated with the virulence attributes. Edc3 is known to be an enhancer of the mRNA decapping reactions and a scaffold protein of cytoplasmic processing bodies (P-bodies). Recent studies of C. albicans Edc3 suggested its critical roles in filamentous growth and stress-induced apoptotic cell death. The edc3/edc3 deletion mutant strain showed increased cell survival and less ROS accumulation upon treatment with hydrogen peroxide. To investigate the diverse involvement of Edc3 in the cellular processes, deletion mutations of LSm, FDF, or YjeF domain of Edc3 were constructed. The edc3-LSmΔ or edc3-YjeFΔ mutation showed the filamentation defect, resistance to oxidative stress, and decreased ROS accumulation. In contrast, the edc3-FDFΔ mutation exhibited a wild-type level of filamentous growth and a mild defect in ROS accumulation. These results suggest that Lsm and YjeF domains of Edc3 are critical in hyphal growth and oxidative stress response.

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Deadenylation and decapping factors cooperatively stimulate biochemical activities of DEAD-box ATPase Dhh1
Gabriel A Braun, Rakesh Kumar, Alan G Hinnebusch, John D Gross
Nucleic Acids Research.2026;[Epub] CrossRef
Roles of P-body factors in Candida albicans filamentation and stress response
Melissa A. Tosiano, Frederick Lanni, Aaron P. Mitchell, C. Joel McManus, Guilhem Janbon
PLOS Genetics.2025; 21(3): e1011632. CrossRef
The FomYjeF Protein Influences the Sporulation and Virulence of Fusarium oxysporum f. sp. momordicae
Chenxing Wei, Caiyi Wen, Yuanyuan Zhang, Hongyan Du, Rongrong Zhong, Zhengzhe Guan, Mengjiao Wang, Yanhong Qin, Fei Wang, Luyang Song, Ying Zhao
International Journal of Molecular Sciences.2023; 24(8): 7260. CrossRef
Intersection of phosphate transport, oxidative stress and TOR signalling in Candida albicans virulence
Ning-Ning Liu, Priya Uppuluri, Achille Broggi, Angelique Besold, Kicki Ryman, Hiroto Kambara, Norma Solis, Viola Lorenz, Wanjun Qi, Maikel Acosta-Zaldívar, S. Noushin Emami, Bin Bao, Dingding An, Francisco A. Bonilla, Martha Sola-Visner, Scott G. Filler,
PLOS Pathogens.2018; 14(7): e1007076. CrossRef
Mutational analysis of metacaspase CaMca1 and decapping activator Edc3 in the pathogenicity of Candida albicans
Jeong-Hoon Jeong, Seok-Eui Lee, Jinmi Kim
Fungal Genetics and Biology.2016; 97: 18. CrossRef

Proteomic Analysis of Hyphae-Specific Proteins That Are Expressed Differentially in cakem1/cakem1 Mutant Strains of Candida albicans: Kang-Hoon Lee , Seung-Yeop Kim , Jong-Hwan Jung , Jinmi Kim; J. Microbiol. 2010;48(3):365-371. Published online June 23, 2010; DOI: https://doi.org/10.1007/s12275-010-9155-4

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The yeast-to-hyphal transition is a major virulence factor in the fungal pathogen Candida albicans. Mutations in the CaKEM1 gene, which encodes a 5′-3′ exoribonuclease responsible for mRNA degradation, show a defect in hyphal growth. We applied two-dimensional gel electrophoresis to identify hyphae-specific proteins that have altered expressions in the presence of the cakem1 mutation. Eight proteins, Eno1, Eps1, Fba1, Imh3, Lpd1, Met6, Pdc11, and Tsa1 were upregulated during hyphal transition in wild-type but not in cakem1/cakem1 mutant cells. A second group of proteins, Idh1, Idh2, and Ssb1, showed increased levels of expression in cakem1/cakem1 mutant cells when compared to wild-type cells. Overexpression of Lpd1, a component of the pyruvate dehydrogenase complex, caused slight hyperfilamentation in a wild-type strain and suppressed the filamentation defect of the cakem1 mutation. The Ssb1 protein, which is a potential heat shock protein, and the Imh3 protein, which is a putative enzyme in GMP biosynthesis also showed the filamentation-associated phenotypes.

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Transcriptomics combined with metabolomics unveiled the key genes and metabolites of mycelium growth in Morchella importuna
Tingting Fan, Rui Ren, Shaojun Tang, Yiyun Zhou, Meng Cai, Wenwen Zhao, Yuelin He, Jun Xu
Frontiers in Microbiology.2023;[Epub] CrossRef
Pathogen-Host Interaction Repertoire at Proteome and Posttranslational Modification Levels During Fungal Infections
Yanjian Li, Hailong Li, Tianshu Sun, Chen Ding
Frontiers in Cellular and Infection Microbiology.2021;[Epub] CrossRef
Epitope-Based Peptide Vaccine Design against Fructose Bisphosphate Aldolase of Candida glabrata: An Immunoinformatics Approach
Lina Mohamed Elamin Elhasan, Mohamed B. Hassan, Reham M. Elhassan, Fatima A. Abdelrhman, Essam A. Salih, Asma Ibrahim H, Amna A. Mohamed, Hozaifa S. Osman, Marwa Saad M. Khalil, Athar A. Alsafi, Abeer Babiker Idris, Mohamed A. Hassan, Roberta Antonia Diot
Journal of Immunology Research.2021; 2021: 1. CrossRef
The evolution of posttranscriptional regulation
Bernhard Schaefke, Wei Sun, Yi‐Sheng Li, Liang Fang, Wei Chen
WIREs RNA.2018;[Epub] CrossRef
The 5′ Untranslated Region of the EFG1 Transcript Promotes Its Translation To Regulate Hyphal Morphogenesis in Candida albicans
Prashant R. Desai, Klaus Lengeler, Mario Kapitan, Silas Matthias Janßen, Paula Alepuz, Ilse D. Jacobsen, Joachim F. Ernst, Aaron P. Mitchell
mSphere.2018;[Epub] CrossRef
Post‐transcriptional gene regulation in the biology and virulence ofCandida albicans
Jiyoti Verma‐Gaur, Ana Traven
Cellular Microbiology.2016; 18(6): 800. CrossRef
Control of Candida albicans morphology and pathogenicity by post-transcriptional mechanisms
David Kadosh
Cellular and Molecular Life Sciences.2016; 73(22): 4265. CrossRef
Roles of dihydrolipoamide dehydrogenase Lpd1 in Candida albicans filamentation
Seung-Yeop Kim, Jinmi Kim
Fungal Genetics and Biology.2010; 47(9): 782. CrossRef

Characterization of Osh3, an Oxysterol-binding Protein, in Filamentous Growth of Saccharomyces cerevisiae and Candida albicans: Hyang-sook Hur , Ji-Ho Ryu , Kwang-Hoon Kim , Jinmi Kim; J. Microbiol. 2006;44(5):523-529.; DOI: https://doi.org/2445 [pii]

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Abstract PDF: OSH3 is one of the seven yeast homologues of the oxysterol binding proteins (OSBPs) which have the major binding affinity to the oxysterols and function as regulator of cholesterol biosynthesis in mammals. Mutational analysis of OSH3 showed that OSH3 plays a regulatory role in the yeast-to-hyphal transition through its oxysterol-binding domain in Saccharomyces cerevisiae. The OSH3 gene was also identified in the pathogenic yeast Candida albicans. Deletion of OSH3 caused a defect in the filamentous growth, which is the major cause of the C. albicans pathogencity. The filamentation defect of the mutation in the MAPK-associated transcription factor, namely cph1Δ was suppressed by overexpression of OSH3. These findings suggest the regulatory roles of OSH3 in the yeast filamentous growth and the functional conservations of OSH3 in S. cerevisiae and C. albicans.

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