Journal of Microbiology

Hyung-Soon Yim

4 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

1,026 View
3 Download
9 Web of Science
7 Crossref

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.

Citations

Citations to this article as recorded by

Fibroblast growth factor homologous factors in neural signaling: Molecular mechanisms and disease-relevant dysregulation
Nanshan Song, Xiangxu Wang, Luqing Ha, Gang Hu
Cytokine & Growth Factor Reviews.2026; 90: 39. CrossRef
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

YlaC is an Extracytoplasmic Function (ECF) Sigma Factor Contributing to Hydrogen Peroxide Resistance in Bacillus subtilis: Han-Bong Ryu , Inji Shin , Hyung-Soon Yim , Sa-Ouk Kang; J. Microbiol. 2006;44(2):206-216.; DOI: https://doi.org/2363 [pii]

570 View
0 Download

Abstract PDF: In this study, we have attempted to characterize the functions of YlaC and YlaD encoded by ylaC and ylaD genes in Bacillus subtilis. The GUS reporter gene, driven by the yla operon promoter, was expressed primarily during the late exponential and early stationary phase, and its expression increased as the result of hydrogen peroxide treatment. Northern and Western blot analyses revealed that the level of ylaC transcripts and YlaC increased as the result of challenge with hydrogen peroxide. A YlaC-overexpressing strain evidenced hydrogen peroxide resistance and a three-fold higher peroxidase activity as compared with a deletion mutant. YlaC-overexpressing and YlaD-disrupted strains evidenced higher sporulation rates than were observed in the YlaC-disrupted and YlaD-overexpressing strains. Analyses of the results of native polyacrylamide gel electrophoresis of recombinant YlaC and YlaD indicated that interaction between YlaC and YlaD was regulated by the redox state of YlaD in vitro. Collectively, the results of this study appear to suggest that YlaC regulated by the YlaD redox state, contribute to oxidative stress resistance in B. subtilis.

Cytochrome c_550 is Related to Initiation of Sporulation in Bacillus subtilis: Inji Shin , Han-Bong Ryu , Hyung-Soon Yim , Sa-Ouk Kang; J. Microbiol. 2005;43(3):244-250.; DOI: https://doi.org/2218 [pii]

535 View
0 Download

Abstract PDF: The effect of cytochrome c_550 encoded by cccA in Bacillus subtilis during the event of sporulation was investigated. The sporulation of cccA-overexpressing mutant was significantly accelerated, while disruptant strain showed delayed sporulation in spite of the same growth rate. Activity of sporulation stage-0-specific enzyme, extracellular [alpha]-amylase of mutant strains was similar to that of the control strain, but cccA-overexpressing mutant exhibited higher activity of stage-II-specific alkaline phosphatase and stage-III-specific glucose dehydrogenase when compared to deletion mutant and control strain. Northern blot analysis also revealed that cccA-overexpressing mutant showed high level of spo0A transcripts, while the disruptant rarely expressed spo0A. These results suggested that although cytochrome c_550 is dispensable for growth and sporulation, expression of cccA may play an important role for initiation of sporulation through regulation of spo0A expression.

Sequence Analysis and Functional Expression of the Structural and Regulatory Genes for Pyruvate Dehydrogenase Complex from Streptomyces seoulensis: Hwan Youn , Jangyul Kwak , Dong-Won Kim , Chang-Jin Lee , Yang-In Yim , Jin-Won Lee , In-Kwon Kim , Jeong-Il Yu , Hyung-Soon Yim , Sa-Ouk Kang; J. Microbiol. 2002;40(1):43-50.

564 View
2 Download

Abstract PDF: A cluster of genes encoding the pyruvate dehydrogenase complex (PDC) of Streptomyces seoulensis, a Gram-positive bacterium, was cloned and sequenced. The genes of S. seoulensis consist of four open reading frames. The first gene, lpd, which encodes a lipoamide dehydrogenase, is followed by pdhB encoding a dihydrolipoamide acetyltransferase (E2p), pdhR, a regulatory gene, and pdhA encoding a pyruvate dehydrogenase component (E1p). E1p had an unusual homodimeric subunit, which has been known only in Gram-negative bacteria. S. seoulensis E2p contains two lipoyl domains like those of humans and Streptococcus faecalis. The pdhR gene appears to be clustered with the structural genes of S. seoulensis PDC. The PdhR-overexpressed S. seoulensis showed growth retardation and the decrease of E1p, indicating that PdhR regulates the function of PDC by repressing the expression of E1p. A strain of Streptomyces lividans overexpressing S. seoulensis PdhR showed a significant decrease in the level of actinorhodin, implying a regulatory role for Streptomyces PDC in antibiotic biosynthesis.

Author index