Journal of Microbiology

Sun-Shin Cha

6 Articles

Expression and purification of intracrine human FGF 11 and study of its FGFR-dependent biological activity: Kyeong Won Lee , Young Jun An , Janet Lee , Ye-Eun Jung , In Young Ko , Jonghwa Jin , Ji Hoon Park , Won Kyu Lee , Kiweon Cha , Sun-Shin Cha , Jung-Hyun Lee , Hyung-Soon Yim; J. Microbiol. 2022;60(11):1086-1094. Published online November 1, 2022; DOI: https://doi.org/10.1007/s12275-022-2406-3

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Fibroblast growth factor 11 (FGF11) is one of intracrine FGFs (iFGFs), which function within cells. Unlike canonical FGFs, FGF11 remains intracellularly and plays biological roles in FGF receptor (FGFR)-independent manner. Here, we established an expression system of recombinant FGF11 proteins in E. coli and investigated whether the extracellular administration of FGF11 can activate cellular signaling. Human FGF11 has two isoforms, FGF11a and FGF11b, depending on the presence of nuclear localization sequences (NLSs) in the N-terminus. Because these two isoforms are unstable, we prepared an FGF11a-Mut by substituting three cysteine residues in the NLS with serine and FGF11b-ΔC with C-terminal truncation. The introduction of mutation in the NLS improved the solubility of FGF11 prepared from E. coli. Exogenous addition of FGF11b and FGF11b-ΔC to BALB3T3 increased cell proliferation, while FGF11a-Mut exerted no effect. FGF11b-ΔC showed higher cell proliferation activity and FGFR signaling than FGF11b. The cell-proliferating activities of FGF11b and FGF11b-ΔC were blocked by an FGFR1 inhibitor or a recombinant FGFR1, confirming the FGFR1- dependent extracellular activity of FGF11b. The analysis of circular dichroism suggested that the C-terminus of FGF11 has an α-helical structure, which may affect its interaction with FGFR1. These results suggest that the N-and C-terminus of recombinant FGF11 are involved in the activation of FGFR1. The above results provide novel insights into the function and mechanism of FGF11 that may aid the development of useful ligands for FGFR regulation.

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Fibroblast Growth Factors: Roles and Emerging Therapeutic Applications
Gaëtane Ternier, Kaynat Shahzad, Oshadi Edirisinghe, Patience Okoto, Zeina Alraawi, Shivakumar Sonnaila, Phuc Phan, Paul D. Adams, Suresh K. Thallapuranam
Current Drug Targets.2025; 26(8): 551. CrossRef
Production and purification of recombinant long protein isoforms of FGF11 subfamily
Martyna Biadun, Szymon Sidor, Marta Kalka, Radoslaw Karelus, Martyna Sochacka, Daniel Krowarsch, Lukasz Opalinski, Malgorzata Zakrzewska
Journal of Biotechnology.2025; 403: 9. CrossRef
Function of orthologous fibroblast growth factor 11 protein in angiogenesis and immunomodulatory after spinal cord injury
Congcong Zou, Min Chen, Qian Zhao, Letong Wang, Luyang Ye, Xiaolei Meng, Xiaokun Li, Yanming Zuo, Zhouguang Wang
International Journal of Biological Macromolecules.2025; 330: 148106. CrossRef
Glycosylation of FGF/FGFR: An underrated sweet code regulating cellular signaling programs
Aleksandra Gędaj, Paulina Gregorczyk, Dominika Żukowska, Aleksandra Chorążewska, Krzysztof Ciura, Marta Kalka, Natalia Porębska, Łukasz Opaliński
Cytokine & Growth Factor Reviews.2024; 77: 39. CrossRef
FGF homologous factors are secreted from cells to induce FGFR‐mediated anti‐apoptotic response
Martyna Biadun, Martyna Sochacka, Radoslaw Karelus, Karolina Baran, Aleksandra Czyrek, Jacek Otlewski, Daniel Krowarsch, Lukasz Opalinski, Malgorzata Zakrzewska
The FASEB Journal.2023;[Epub] CrossRef
FGF/FGFR1 system in paired breast tumor-adjacent and tumor tissues, associations with mammographic breast density and tumor characteristics
Öykü Boraka, Marie Klintman, Johan Vallon-Christersson, Sophia Zackrisson, Per Hall, Signe Borgquist, Ann H. Rosendahl
Frontiers in Oncology.2023;[Epub] CrossRef

Purification, crystallization, and preliminary X-ray crystallographic analysis of the Group III chaperonin from Carboxydothermus hydrogenoformans: Young Jun An , Sara E. Rowland , Frank T. Robb , Sun-Shin Cha; J. Microbiol. 2016;54(6):440-444. Published online May 27, 2016; DOI: https://doi.org/10.1007/s12275-016-6089-5

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Chaperonins (CPNs) are megadalton sized ATP-dependent nanomachines that facilitate protein folding through complex cycles of complex allosteric articulation. They consist of two back-to-back stacked multisubunit rings. CPNs are usually classified into Group I and Group II. Here, we report the crystallization of both the AMPPNP (an ATP analogue) and ADP bound forms of a novel CPN, classified as belonging to a third Group, recently discovered in the extreme thermophile Carboxydothermus hydrogenoformans. Crystals of the two forms were grown by the vapor batch crystallization
method
at 295 K. Crystals of the Ch-CPN/AMPPNP complex diffracted to 3.0 Å resolution and belonged to the space group P422, with unit-cell parameters a = b = 186.166, c = 160.742 Å. Assuming the presence of four molecules in the asymmetric unit, the solvent content was estimated to be about 60.02%. Crystals of the Ch-CPN/ADP complex diffracted to 4.0 Å resolution and belonged to the space group P4212, with unit-cell parameters a = b = 209.780, c = 169.813Å. Assuming the presence of four molecules in the asymmetric unit, the solvent content was estimated to be about 70.19%.

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Bridging human chaperonopathies and microbial chaperonins
Everly Conway de Macario, Masafumi Yohda, Alberto J. L. Macario, Frank T. Robb
Communications Biology.2019;[Epub] CrossRef
Prokaryotic Chaperonins as Experimental Models for Elucidating Structure-Function Abnormalities of Human Pathogenic Mutant Counterparts
Everly Conway de Macario, Frank T. Robb, Alberto J. L. Macario
Frontiers in Molecular Biosciences.2017;[Epub] CrossRef
Structural and mechanistic characterization of an archaeal-like chaperonin from a thermophilic bacterium
Young Jun An, Sara E. Rowland, Jung-Hyun Na, Dario Spigolon, Seung Kon Hong, Yeo Joon Yoon, Jung-Hyun Lee, Frank T. Robb, Sun-Shin Cha
Nature Communications.2017;[Epub] CrossRef

The crystal structure of the D-alanine-D-alanine ligase from Acinetobacter baumannii suggests a flexible conformational change in the central domain before nucleotide binding: Kim-Hung Huynh , Myoung-ki Hong , Clarice Lee , Huyen-Thi Tran , Sang Hee Lee , Yeh-Jin Ahn , Sun-Shin Cha , Lin-Woo Kang; J. Microbiol. 2015;53(11):776-782. Published online October 28, 2015; DOI: https://doi.org/10.1007/s12275-015-5475-8

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Acinetobacter baumannii, which is emerging as a multidrugresistant nosocomial pathogen, causes a number of diseases, including pneumonia, bacteremia, meningitis, and skin infections. With ATP hydrolysis, the D-alanine-D-alanine ligase (DDL) catalyzes the synthesis of D-alanyl-D-alanine, which is an essential component of bacterial peptidoglycan. In this study, we determined the crystal structure of DDL from A. baumannii (AbDDL) at a resolution of 2.2 Å. The asymmetric unit contained six protomers of AbDDL. Five protomers had a closed conformation in the central domain, while one protomer had an open conformation in the central domain. The central domain with an open conformation did not interact with crystallographic symmetry-related protomers and the conformational change of the central domain was not due to crystal packing. The central domain of AbDDL can have an ensemble of the open and closed conformations before the binding of substrate ATP. The conformational change of the central domain is important for the catalytic activity and the detail information will be useful for the development of inhibitors against AbDDL and putative antibacterial agents against A. baumannii. The AbDDL structure was compared with that of other DDLs that were in complex with potent inhibitors and the catalytic activity of AbDDL was confirmed using enzyme kinetics assays.

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In Silico Design and In Vitro Assessment of Bicyclic Trifluoromethylated Pyrroles as New Antibacterial and Antifungal Agents
Diana Hodyna, Anton Klipkov, Maryna Kachaeva, Yurii Shulha, Igor Gerus, Larysa Metelytsia, Vasyl Kovalishyn
Chemistry & Biodiversity.2024;[Epub] CrossRef
Genome-Scale Metabolic Modeling Reveals Metabolic Alterations of Multidrug-Resistant Acinetobacter baumannii in a Murine Bloodstream Infection Model
Jinxin Zhao, Yan Zhu, Jiru Han, Yu-Wei Lin, Michael Aichem, Jiping Wang, Ke Chen, Tony Velkov, Falk Schreiber, Jian Li
Microorganisms.2020; 8(11): 1793. CrossRef
Identification of natural inhibitors against Acinetobacter baumannii d-alanine-d-alanine ligase enzyme: A multi-spectrum in silico approach
Sajjad Ahmad, Saad Raza, Sumra Wajid Abbasi, Syed Sikander Azam
Journal of Molecular Liquids.2018; 262: 460. CrossRef
Molecular characterization of SCO0765 as a cellotriose releasing endo-β-1,4-cellulase from Streptomyces coelicolor A(3)
Joo-Bin Hong, Vijayalakshmi Dhakshnamoorthy, Chang-Ro Lee
Journal of Microbiology.2016; 54(9): 626. CrossRef

Structural basis for the ATP-independent proteolytic activity of LonB proteases and reclassification of their AAA+ modules: Young Jun An , Jung-Hyun Na , Myung-Il Kim , Sun-Shin Cha; J. Microbiol. 2015;53(10):711-717. Published online October 2, 2015; DOI: https://doi.org/10.1007/s12275-015-5417-5

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Lon proteases degrade defective or denature proteins as well as some folded proteins for the control of cellular protein quality. There are two types of Lon proteases, LonA and LonB. Each consists of two functional components: a protease component and an ATPase associated with various cellular activities (AAA+ module). Here, we report the 2.03 Å-resolution crystal structure of the isolated AAA+ module (iAAA+ module) of LonB from Thermococcus onnurineus NA1 (TonLonB). The iAAA+ module, having no bound nucleotide, adopts a conformation virtually identical to the ADP-bound conformation of AAA+ modules in the hexameric structure of TonLonB; this provides insights into the ATP-independent proteolytic activity observed in a LonB protease. Structural comparison of AAA+ modules between LonA and LonB revealed that the AAA+ modules of Lon proteases are separated into two distinct clades depending on their structural features. The AAA+ module of LonB belongs to the ‘H2 & Ins1 insert clade (HINS clade)’ defined for the first time in this study, while the AAA+ module of LonA is a member of the HCLR clade.

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Unique Structural Fold of LonBA Protease from Bacillus subtilis, a Member of a Newly Identified Subfamily of Lon Proteases
Alla Gustchina, Mi Li, Anna G. Andrianova, Arsen M. Kudzhaev, George T. Lountos, Bartosz Sekula, Scott Cherry, Joseph E. Tropea, Ivan V. Smirnov, Alexander Wlodawer, Tatyana V. Rotanova
International Journal of Molecular Sciences.2022; 23(19): 11425. CrossRef
Structure and the Mode of Activity of Lon Proteases from Diverse Organisms
Alexander Wlodawer, Bartosz Sekula, Alla Gustchina, Tatyana V. Rotanova
Journal of Molecular Biology.2022; 434(7): 167504. CrossRef
Proteolytic systems of archaea: slicing, dicing, and mincing in the extreme
Nicholas P. Robinson, Julie A. Maupin-Furlow
Emerging Topics in Life Sciences.2018; 2(4): 561. CrossRef

Author’s Correction] Experimental Phasing Using Zinc and Sulfur Anomalous Signals Measured at the Zinc Absorption Peak: Sangmin Lee , Min-Kyu Kim , Chang-Jun Ji , Jin-Won Lee , Sun-Shin Cha; J. Microbiol. 2013;51(6):886-886.; DOI: https://doi.org/10.1007/s12275-013-0725-5

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Abstract PDF: In the article by Lee et al. published in the Journal of Microbiology 2013; 51, 639-643. Acknowledgement should appear as shown below. This work was supported by the National Research Foundation of Korea Grant NRF-2012R1A2A2A02005978, the CAP through Korea Research Council of Fundamental Science Technology (KRCF), Korea Institute of Science and Technology (KIST), & Korea Institute of Ocean Science and Technology (KIOST), the Marine and Extreme Genome Research Center program, and the Development of Biohydrogen Production Technology Using Hyperthermophilic Archaea program of MOF. Works performed at Hanyang University were supported by Basic Science Research Program through the National Research Foundation of Korea (NRF) funded by the Ministry of Education, Science and Technology (MEST) (KRF-2008-313-C00774).

Experimental Phasing Using Zinc and Sulfur Anomalous Signals Measured at the Zinc Absorption Peak: Sangmin Lee , Min-Kyu Kim , Chang-Jun Ji , Jin-Won Lee , Sun-Shin Cha; J. Microbiol. 2013;51(5):639-643. Published online October 31, 2013; DOI: https://doi.org/10.1007/s12275-013-3412-2

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Abstract PDF: Iron is an essential transition metal required for bacterial growth and survival. Excess free iron can lead to the generation of reactive oxygen species that can cause severe damage to cellular functions. Cells have developed iron-sensing regulators to maintain iron homeostasis at the transcription level. The ferric uptake regulator (Fur) is an iron-responsive regulator that controls the expression of genes involved in iron homeostasis, bacterial virulence, stress resistance, and redox metabolism. Here, we report the expression, purification, crystallization, and phasing of the apo-form of Bacillus subtilis Fur (BsFur) in the absence of regulatory metal ions. Crystals were obtained by microbatch crystallization method at 295 K and diffraction data at a resolution of 2.6 Å was collected at the zinc peak wavelength (λ=1.2823 Å). Experimental phasing identified the positions of one zinc atom and four sulfur atoms of cysteine residues coordinating the zinc atom, indicating that the data contained a meaningful anomalous scattering originating from the ordered zinc-coordinating sulfur atoms, in spite of the small anomalous signals of sulfur atoms at the examined wavelength.

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