Journal of Microbiology

Inseong Jo

5 Articles

Structural and Functional Analyses of the Flavoprotein Disulfide Reductase FN0820 of Fusobacterium nucleatum: Hyunwoo Shin , Yeongjin Baek , Dukwon Lee , Yongbin Xu , Yonghoon Kwon , Inseong Jo , Nam-Chul Ha; J. Microbiol. 2023;61(12):1033-1041. Published online December 20, 2023; DOI: https://doi.org/10.1007/s12275-023-00095-9

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Escherichia coli RclA and Staphylococcus aureus MerA are part of the Group I flavoprotein disulfide reductase (FDR) family and have been implicated in the contribution to bacterial pathogenesis by defending against the host immune response. Fusobacterium nucleatum is a pathogenic, anaerobic Gram-negative bacterial species commonly found in the human oral cavity and gastrointestinal tract. In this study, we discovered that the F. nucleatum protein FN0820, belonging to the Group I FDR family, exhibited a higher activity of a Cu2+- dependent NADH oxidase than E. coli RclA. Moreover, FN0820 decreased the dissolved oxygen level in the solution with higher NADH oxidase activity. We found that L-tryptophan and its analog 5-hydroxytryptophan inhibit the FN0820 activities of NADH oxidase and the concomitant reduction of oxygen. Our results have implications for developing new treatment strategies against pathogens that defend the host immune response with Group I FDRs.

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The role of metals in hypothiocyanite resistance in Escherichia coli
Michael J. Gray, Laurie E. Comstock
Journal of Bacteriology.2024;[Epub] CrossRef

Crystal structure of the phage-encoded N-acetyltransferase in complex with acetyl-CoA, revealing a novel dimeric arrangement: Nayeon Ki , Inseong Jo , Yongseong Hyun , Jinwook Lee , Nam-Chul Ha , Hyun-Myung Oh; J. Microbiol. 2022;60(7):746-755. Published online July 4, 2022; DOI: https://doi.org/10.1007/s12275-022-2030-2

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Abstract PDF

Bacteriophages employ diverse mechanisms to facilitate the proliferation of bacteriophages. The Salmonella-infecting phage SPN3US contains a putative N-acetyltransferase, which is widely found in bacteriophages. However, due to low sequence similarity to the N-acetyltransferases from bacteria and eukaryotic cells, the structure and function of phage-encoded acetyltransferases are mainly unknown. This study determines the crystal structure of the putative N-acetyltransferase of SPN3US in complex with acetyl-CoA. The crystal structure showed a novel homodimeric arrangement stabilized by exchanging the C-terminal α-helix within the dimer. The following biochemical analyses suggested that the phageencoded acetyltransferase might have a very narrow substrate specificity. Further studies are required to reveal the biochemical activity, which would help elucidate the interaction between the phage and host bacteria in controlling pathogenic bacteria.

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Characteristics of the smallest brucellaphage with strong lytic ability
Hongbaiyu Liu, Youhong Zhong, Zhihong Zhang, Kehong Xu, Chunpeng Mao, Qiuju Yang, Lihua Yang, Binbin Yu, Ying Long, Xinyu Qin, Liyuan Shi, Sheng Chang, Yuanying Shen, Peng Wang
Frontiers in Veterinary Science.2025;[Epub] CrossRef
Structural basis for Salmonella infection by two Microviridae phages
Wanlong Hu, Zhengjie Liu, Yuming Wei, Qucheng Bian, Weiqi Lan, Chongzheng Fan, Jiaoyang Song, Qianqian Sun, Xiaojie Zhang, Yuqing Liu, Yan Gao, Yibao Chen
Communications Biology.2025;[Epub] CrossRef
Posttranslational modifications in bacteria during phage infection
Hannelore Longin, Nand Broeckaert, Vera van Noort, Rob Lavigne, Hanne Hendrix
Current Opinion in Microbiology.2024; 77: 102425. CrossRef

Crystal structure of the nuclease and capping domain of SbcD from Staphylococcus aureus: Jinwook Lee , Inseong Jo , Jinsook Ahn , Seokho Hong , Soyeon Jeong , Aeran Kwon , Nam-Chul Ha; J. Microbiol. 2021;59(6):584-589. Published online April 20, 2021; DOI: https://doi.org/10.1007/s12275-021-1012-0

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Abstract PDF

The SbcCD complex is an essential component of the DNA double-strand break (DSB) repair system in bacteria. The bacterial SbcCD complex recognizes and cleaves the DNA ends in DSBs by ATP-dependent endo- and exonuclease activities as an early step of the DNA repair process. SbcD consists of nuclease, capping, and helix-loop-helix domains. Here, we present the crystal structure of a SbcD fragment from Staphylococcus aureus, which contained nuclease and capping domains, at a resolution of 2.9 Å. This structure shows a dimeric assembly similar to that of the corresponding domains of SbcD from Escherichia coli. The S. aureus SbcD fragment exhibited endonuclease activities on supercoiled DNA and exonuclease activity on linear and nicked DNA. This study contributes to the understanding of the molecular basis for how bacteria can resist sterilizing treatment, causing DNA damage.

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A Cas12a Toolbox for Rapid and Flexible Group B Streptococcus Genomic Editing and CRISPRi
G. H. Hillebrand, S. C. Carlin, E. J. Giacobe, H. A. Stephenson, J. Collins, T. A. Hooven
Molecular Microbiology.2025; 124(5): 449. CrossRef
Solvent-polarity-programmed chirality transfer in stereodiversified dipeptide-based self-assembly system with light-responsive circular dichroism property
Minghao Wang, Hanting Wang, Shunjie Cheng, Yuanyuan Wang, Lukang Ji
Colloids and Surfaces A: Physicochemical and Engineering Aspects.2025; 726: 137897. CrossRef
Molecular characterisation of Toxoplasma gondii Mre11 reveals unique structural features and potential as a therapeutic target
Diego M. Ruiz, Valeria R. Turowski, William J. Sullivan, Sergio O. Angel
Scientific Reports.2025;[Epub] CrossRef
Staphylococcus aureus SOS response: Activation, impact, and drug targets
Kaiying Cheng, Yukang Sun, Huan Yu, Yingxuan Hu, Yini He, Yuanyuan Shen
mLife.2024; 3(3): 343. CrossRef

Recent paradigm shift in the assembly of bacterial tripartite efflux pumps and the type I secretion system: Inseong Jo , Jin-Sik Kim , Yongbin Xu , Jaekyung Hyun , Kangseok Lee , Nam-Chul Ha; J. Microbiol. 2019;57(3):185-194. Published online February 26, 2019; DOI: https://doi.org/10.1007/s12275-019-8520-1

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Abstract PDF

Tripartite efflux pumps and the type I secretion system of Gram-negative bacteria are large protein complexes that span the entire cell envelope. These complexes expel antibiotics and other toxic substances or transport protein toxins from bacterial cells. Elucidating the binary and ternary complex structures at an atomic resolution are crucial to understanding the assembly and working mechanism. Recent advances in cryoelectron microscopy along with the construction of chimeric proteins drastically shifted the assembly models. In this review, we describe the current assembly models from a historical perspective and emphasize the common assembly mechanism for the assembly of diverse tripartite pumps and type I secretion systems.

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Molecular Insights into CLD Domain Dynamics and Toxin Recruitment of the HlyA E. coli T1SS
Rocco Gentile, Stephan Schott-Verdugo, Sakshi Khosa, Cigdem Günes, Michele Bonus, Jens Reiners, Sander H.J. Smits, Lutz Schmitt, Holger Gohlke
Journal of Molecular Biology.2025; 437(24): 169485. CrossRef
Molecular mechanisms of antibiotic resistance revisited
Elizabeth M. Darby, Eleftheria Trampari, Pauline Siasat, Maria Solsona Gaya, Ilyas Alav, Mark A. Webber, Jessica M. A. Blair
Nature Reviews Microbiology.2023; 21(5): 280. CrossRef
Permeation of Fosfomycin through the Phosphate-Specific Channels OprP and OprO of Pseudomonas aeruginosa
Vinaya Kumar Golla, Claudio Piselli, Ulrich Kleinekathöfer, Roland Benz
The Journal of Physical Chemistry B.2022; 126(7): 1388. CrossRef
Adaptation of the periplasm to maintain spatial constraints essential for cell envelope processes and cell viability
Eric Mandela, Christopher J Stubenrauch, David Ryoo, Hyea Hwang, Eli J Cohen, Von L Torres, Pankaj Deo, Chaille T Webb, Cheng Huang, Ralf B Schittenhelm, Morgan Beeby, JC Gumbart, Trevor Lithgow, Iain D Hay
eLife.2022;[Epub] CrossRef
Structure, Assembly, and Function of Tripartite Efflux and Type 1 Secretion Systems in Gram-Negative Bacteria
Ilyas Alav, Jessica Kobylka, Miriam S. Kuth, Klaas M. Pos, Martin Picard, Jessica M. A. Blair, Vassiliy N. Bavro
Chemical Reviews.2021; 121(9): 5479. CrossRef
Biotechnological applications of type 1 secretion systems
Zohreh Pourhassan N., Sander H.J. Smits, Jung Hoon Ahn, Lutz Schmitt
Biotechnology Advances.2021; 53: 107864. CrossRef
Protein-Protein Interactions in the Cytoplasmic Membrane of Escherichia coli: Influence of the Overexpression of Diverse Transporter-Encoding Genes on the Activities of PTS Sugar Uptake Systems
Mohammad Aboulwafa, Zhongge Zhang, Milton H. Saier Jr.
Microbial Physiology.2020; 30(1-6): 36. CrossRef
Perspectives towards antibiotic resistance: from molecules to population
Joon-Hee Lee
Journal of Microbiology.2019; 57(3): 181. CrossRef

Crystal structure of Streptomyces coelicolor RraAS2, an unusual member of the RNase E inhibitor RraA protein family: Nohra Park , Jihune Heo , Saemee Song , Inseong Jo , Kangseok Lee , Nam-Chul Ha; J. Microbiol. 2017;55(5):388-395. Published online April 29, 2017; DOI: https://doi.org/10.1007/s12275-017-7053-8

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Abstract PDF

Bacterial ribonuclease E (RNase E) plays a crucial role in the processing and decay of RNAs. A small protein named RraA negatively regulates the activity of RNase E via protein-protein interaction in various bacteria. Recently, RraAS1 and RraAS2, which are functional homologs of RraA from Escherichia coli, were identified in the Gram-positive species Streptomyces coelicolor. RraAS1 and RraAS2 inhibit RNase ES ribonuclease activity in S. coelicolor. RraAS1 and RraAS2 have a C-termi-nal extension region unlike typical bacterial RraA proteins. In this study, we present the crystal structure of RraAS2, ex-hibiting a hexamer arranged in a dimer of trimers, consistent with size exclusion chromatographic results. Importantly, the C-terminal extension region formed a long α-helix at the junction of the neighboring subunit, which is similar to the trimeric RraA orthologs from Saccharomyces cerevisiae. Trun-cation of the C-terminal extension region resulted in loss of RNase ES inhibition, demonstrating its crucial role. Our find-ings present the first bacterial RraA that has a hexameric assembly with a C-terminal extension α-helical region, which plays an essential role in the regulation of RNase ES activity in S. coelicolor.

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S267P mutation of OxyR regulator in Zymomonas mobilis: mechanism of oxidative stress tolerance and applications in cellulosic hydrolysate fermentation and oxidative stress monitoring
Yi Wang, Binan Geng, Shuyi Liu, Yalun Wu, Shihui Yang
Synthetic and Systems Biotechnology.2026; 13: 531. CrossRef
Relaxed Cleavage Specificity of Hyperactive Variants of Escherichia coli RNase E on RNA I
Dayeong Bae, Hana Hyeon, Eunkyoung Shin, Ji-Hyun Yeom, Kangseok Lee
Journal of Microbiology.2023; 61(2): 211. CrossRef
An oxidative metabolic pathway of 4-deoxy-L-erythro-5-hexoseulose uronic acid (DEHU) from alginate in an alginate-assimilating bacterium
Ryuji Nishiyama, Takao Ojima, Yuki Ohnishi, Yasuhiro Kumaki, Tomoyasu Aizawa, Akira Inoue
Communications Biology.2021;[Epub] CrossRef
The coordinated action of RNase III and RNase G controls enolase expression in response to oxygen availability in Escherichia coli
Minho Lee, Minju Joo, Minji Sim, Se-Hoon Sim, Hyun-Lee Kim, Jaejin Lee, Minkyung Ryu, Ji-Hyun Yeom, Yoonsoo Hahn, Nam-Chul Ha, Jang-Cheon Cho, Kangseok Lee
Scientific Reports.2019;[Epub] CrossRef
RNase G controls tpiA mRNA abundance in response to oxygen availability in Escherichia coli
Jaejin Lee, Dong-Ho Lee, Che Ok Jeon, Kangseok Lee
Journal of Microbiology.2019; 57(10): 910. CrossRef
Functional implications of hexameric assembly of RraA proteins from Vibrio vulnificus
Saemee Song, Seokho Hong, Jinyang Jang, Ji-Hyun Yeom, Nohra Park, Jaejin Lee, Yeri Lim, Jun-Yeong Jeon, Hyung-Kyoon Choi, Minho Lee, Nam-Chul Ha, Kangseok Lee, Eric Cascales
PLOS ONE.2017; 12(12): e0190064. CrossRef

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