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Jong-Soon Choi 5 Articles
Directed analysis of cyanobacterial membrane phosphoproteome using stained phosphoproteins and titanium-enriched phosphopeptides§
Dong-Gi Lee , Joseph Kwon , Chi-Yong Eom , Young-Moon Kang , Seong Woon Roh , Kyung-Bok Lee , Jong-Soon Choi
J. Microbiol. 2015;53(4):279-287.   Published online April 8, 2015
DOI: https://doi.org/10.1007/s12275-015-5021-8
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AbstractAbstract PDF
Gel-free shotgun phosphoproteomics of unicellular cyanobacterium Synechocystis sp. PCC 6803 has not been reported up to now. The purpose of this study is to develop directed membrane phosphoproteomic method in Synechocystis sp. Total Synechocystis membrane proteins were separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and phosphoprotein-stained gel bands were selectively subjected to in-gel trypsin digestion. The phosphorylation sites of the resulting peptides were determined by assigning the neutral loss of [M-H3PO4] to Ser, Thr, and Tyr residues using nano-liquid chromatography 7 Tesla Fourier transform mass spectrometry. As an initial application, 111 proteins and 33 phosphoproteins were identified containing 11 integral membrane proteins. Identified four unknown phosphoproteins with transmembrane helices were suggested to be involved in membrane migration or transporters based on BLASTP search annotations. The overall distribution of hydrophobic amino acids in pTyr was lower in frequency than that of pSer or pThr. Positively charged amino acids were abundantly revealed in the surrounding amino acids centered on pTyr. A directed shotgun membrane phosphoproteomic strategy provided insight into understanding the fundamental regulatory processes underlying Ser, Thr, and Tyr phosphorylation in multi-layered membranous cyanobacteria.

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  • Global Profiling of Protein Phosphorylation, Acetylation, and β-Hydroxybutyrylation in Nannochloropsis oceanica
    Lingyu Ouyang, Wuxin You, Ansgar Poetsch, Li Wei
    Journal of Agricultural and Food Chemistry.2024; 72(47): 26248.     CrossRef
  • Post-translational Modifications of Serine/Threonine and Histidine Kinases and Their Roles in Signal Transductions in Synechocystis Sp. PCC 6803
    Wu Xu, Yingchun Wang
    Applied Biochemistry and Biotechnology.2021; 193(3): 687.     CrossRef
  • Comprehensive Phosphoproteomic Analysis of Nostoc flagelliforme in Response to Dehydration Provides Insights into Plant ROS Signaling Transduction
    Wenyu Liang, Fengkun Yan, Meng Wang, Xiaoxu Li, Zheng Zhang, Xiaorong Ma, Jinhong Hu, Jun Wang, Lingxia Wang
    ACS Omega.2021; 6(21): 13554.     CrossRef
  • Metaproteomic analysis of harmful algal bloom in the Daechung reservoir, Korea
    Jong-Soon Choi, Yun Hwan Park, Soo Hyeon Kim, Ju Seong Park, Yoon-E Choi
    Environmental Biology Research.2020; 38(3): 424.     CrossRef
  • Efficient profiling of detergent-assisted membrane proteome in cyanobacteria
    Jong-Soon Choi, Yun Hwan Park, Jeong Hyun Oh, Sooyong Kim, Joseph Kwon, Yoon-E Choi
    Journal of Applied Phycology.2020; 32(2): 1177.     CrossRef
  • Assessment of Protein Content and Phosphorylation Level in Synechocystis sp. PCC 6803 under Various Growth Conditions Using Quantitative Phosphoproteomic Analysis
    Masakazu Toyoshima, Yuma Tokumaru, Fumio Matsuda, Hiroshi Shimizu
    Molecules.2020; 25(16): 3582.     CrossRef
  • Proteomic De-Regulation in Cyanobacteria in Response to Abiotic Stresses
    Piyoosh Kumar Babele, Jay Kumar, Venkatesh Chaturvedi
    Frontiers in Microbiology.2019;[Epub]     CrossRef
  • The S-layer biogenesis system of Synechocystis 6803: Role of Sll1180 and Sll1181 (E. coli HlyB and HlyD analogs) as type-I secretion components for Sll1951 export
    Rachna Agarwal, Julian P. Whitelegge, Sanjay Saini, Amit Prakash Shrivastav
    Biochimica et Biophysica Acta (BBA) - Biomembranes.2018; 1860(7): 1436.     CrossRef
  • Proteomics of cyanobacteria: current horizons
    Natalia Battchikova, Dorota Muth-Pawlak, Eva-Mari Aro
    Current Opinion in Biotechnology.2018; 54: 65.     CrossRef
  • Determination of the Role of Microcystis aeruginosa in Toxin Generation Based on Phosphoproteomic Profiles
    Jiangqi Qu, Liping Shen, Meng Zhao, Wentong Li, Chengxia Jia, Hua Zhu, Qingjing Zhang
    Toxins.2018; 10(7): 304.     CrossRef
  • Functional Diversity of Transcriptional Regulators in the Cyanobacterium Synechocystis sp. PCC 6803
    Mengliang Shi, Xiaoqing Zhang, Guangsheng Pei, Lei Chen, Weiwen Zhang
    Frontiers in Microbiology.2017;[Epub]     CrossRef
  • Proteomic analysis of post translational modifications in cyanobacteria
    Qian Xiong, Zhuo Chen, Feng Ge
    Journal of Proteomics.2016; 134: 57.     CrossRef
  • Proteomic and metabolomic analyses reveal metabolic responses to 3-hydroxypropionic acid synthesized internally in cyanobacterium Synechocystis sp. PCC 6803
    Yunpeng Wang, Lei Chen, Weiwen Zhang
    Biotechnology for Biofuels.2016;[Epub]     CrossRef
Analysis of Cytoplasmic Membrane Proteome of Streptococcus pneumoniae by Shotgun Proteomic Approach
Chi-Won Choi , Sung-Ho Yun , Sang-Oh Kwon , Sun-Hee Leem , Jong-Soon Choi , Chi-Young Yun , Seung Il Kim
J. Microbiol. 2010;48(6):872-876.   Published online January 9, 2011
DOI: https://doi.org/10.1007/s12275-010-0220-9
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AbstractAbstract PDF
In this study, cytoplasmic membrane proteins of S. pneumoniae strain R6 (ATCC BBA-255) were effectively separated from cell wall or extracellular proteins by sodium carbonate precipitation (SCP) and ultracentrifugation. Forty seven proteins were analyzed as cytoplasmic membrane proteins from the 260 proteins identified by the shotgun proteomic method using SDS-PAGE/LC/MS-MS. ABC transporters for metabolites such as metals, oligopeptides, phosphate, sugar, and amino acids, and membrane proteins involved in phosphotransferse systems, were identified as the predominant and abundant, cytoplasmic membrane proteins that would be essential for nutrient uptake, antibiotic resistance and virulence mechanisms. Our result supports that gel-based shotgun proteomics combined with sodium carbonate precipitation and ultracentrifugation is an effective method for analysis of cytoplasmic membrane proteins of S. pneumoniae.

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  • Efficient profiling of detergent-assisted membrane proteome in cyanobacteria
    Jong-Soon Choi, Yun Hwan Park, Jeong Hyun Oh, Sooyong Kim, Joseph Kwon, Yoon-E Choi
    Journal of Applied Phycology.2020; 32(2): 1177.     CrossRef
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    Artificial Organs.2012; 36(8): 724.     CrossRef
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    Xiao-Yan Yang, Jie Lu, Xuesong Sun, Qing-Yu He
    Journal of Proteomics.2012; 75(10): 2803.     CrossRef
  • Analysis of Streptococcus pneumoniae secreted antigens by immuno-proteomic approach
    Chi-Won Choi, Yeol Gyun Lee, Sang-Oh Kwon, Hye-Yeon Kim, Je Chul Lee, Young-Ho Chung, Chi-Young Yun, Seung Il Kim
    Diagnostic Microbiology and Infectious Disease.2012; 72(4): 318.     CrossRef
Proteomic Analysis of Outer Membrane Proteins from Acinetobacter baumannii DU202 in Tetracycline Stress Condition
Sung-Ho Yun , Chi-Won Choi , Soon-Ho Park , Je Chul Lee , Sun-Hee Leem , Jong-Soon Choi , Soohyun Kim , Seung Il Kim
J. Microbiol. 2008;46(6):720-727.   Published online December 24, 2008
DOI: https://doi.org/10.1007/s12275-008-0202-3
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AbstractAbstract PDF
Acinetobacter baumannii readily developed antimicrobial resistance to clinically available antibiotics. A. baumannii DU202 is a multi-drug resistant strain, and is highly resistant to tetracycline (MIC>1,024μg/ml). The surface proteome of A. baumannii DU202 in response to the sub-minimal inhibitory concentration (subMIC) of tetracycline was analyzed by 2-DE/MS-MS and 1-DE/LC/MS-MS to understand the pathways that form barriers for tetracycline. Membrane expression of major outer membrane proteins (Omps) was significantly decreased in response to the subMIC of tetracycline. These Omps with sizes of 38, 32, 28, and 21 kDa were identified as OmpA38, OmpA32, CarO, and OmpW, respectively. However, transcription level of these Omps was not significantly changed. 1-DE/LC/MS-MS analysis of secreted proteins showed that OmpA38, CarO, OmpW, and other Omps were increasingly secreted at tetracycline condition. This result suggests that A. baumannii actively regulates the membrane expression and the secretion of Omps to overcome antibiotic stress condition.

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    Journal of Applied Phycology.2020; 32(2): 1177.     CrossRef
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Cyanobacterial Hybrid Kinase Sll0043 Regulates Phototaxis by Suppressing Pilin and Twitching Motility Protein
Bong-Jeong Shin , Jeehyun Oh , Sungsoo Kang , Young-Ho Chung , Young Mok Park , Young Hwan Kim , Seungil Kim , Jong Bhak , Jong-Soon Choi
J. Microbiol. 2008;46(3):300-308.   Published online July 5, 2008
DOI: https://doi.org/10.1007/s12275-007-0212-6
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AbstractAbstract PDF
The unicellular cyanobacterium Synechocystis sp. PCC 6803 glides toward a light source through the interplay of positive phototaxis genes and proteins. In genetic analysis, the complete disruption of the hybrid sensory kinase sll0043 produced negative phototaxis. Furthermore, Sll0043 was found to be a hub protein by in silico prediction of protein-protein interaction, in which Sll0043 was predominantly linked to seven two-component proteins with high confidence. To understand the regulation and networking of positive phototaxis proteins, the proteomic profile of the sll0043 mutant was compared to that of wild-type. In the sll0043 mutant, 18 spots corresponding to 15 unique proteins were altered by 1.3 to 59 fold; the spots were identified by 2-DE/MALDI-MS analysis. Down-regulated proteins in the sll0043 null-mutant included chaperonins, superoxide dismutase, and phycocyanin β-subunit. In contrast, nine proteins involved in photosynthesis, translation, regulatory function, and other functions were up-regulated. In particular, a twitching motility protein (PilT1) was induced over 2-fold in sll0043 mutant. Moreover, semiquantitative and quantitative RT-PCR analysis revealed that pilin (pilA1), pili motor (pilT1), and pili switch gene (pilT2) were significantly increased in sll0043 mutant. These results suggest that the hybrid kinase Sll0043 regulates positive phototaxis by suppressing the expression of pili biosynthesis and regulatory genes and through the interplay with positive phototaxis/motility two-component proteins.

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Cloning and Sequence Analysis of Two Catechol-degrading Gene Clusters from a Phenol-utilizing Bacterium Pseudomonas putida SM25
Young-Hee Jung , Jong-Ok Ka , Choong-Ill Cheon , Myeong-Sok Lee , Eun-Sook Song , Soon-Young Choi , Daeho Cho , Sang-Ho Choi , Kwon-Soo Ha , Young Mok Park , Jong-Soon Choi , Kyung-Hee Min
J. Microbiol. 2003;41(2):102-108.
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A 6.1 kb Sph I fragment from the genomic DNA of Pseudomonas putida SM 25 was cloned into the vector pUC19. The open reading frame of catB was found to consist of 1,122 nucleotides. The sequence alignment of the catB gene products from different kinds of bacteria revealed an overall identity ranging from 40 to 98%. The catC gene contained an open reading frame of 96 codons, from which a protein with a molecular mass of about 10.6 kDa was predicted. The amino acids in the proposed activesite region of CatC were found to be almost conserved, including the charged residues. Since the catBC genes in P. putida SM25 were tightly linked, they could be regulated under coordinate transcription, and transcribed from a single promoter located upstream of the catB gene, as in P. putida RB1.

Journal of Microbiology : Journal of Microbiology
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