- Directed analysis of cyanobacterial membrane phosphoproteome using stained phosphoproteins and titanium-enriched phosphopeptides§
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Dong-Gi Lee , Joseph Kwon , Chi-Yong Eom , Young-Moon Kang , Seong Woon Roh , Kyung-Bok Lee , Jong-Soon Choi
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J. Microbiol. 2015;53(4):279-287. Published online April 8, 2015
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DOI: https://doi.org/10.1007/s12275-015-5021-8
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917
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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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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
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Chi-Won Choi , Sung-Ho Yun , Sang-Oh Kwon , Sun-Hee Leem , Jong-Soon Choi , Chi-Young Yun , Seung Il Kim
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J. Microbiol. 2010;48(6):872-876. Published online January 9, 2011
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DOI: https://doi.org/10.1007/s12275-010-0220-9
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709
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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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Chi-Won Choi, Hee-Young An, Yong Ju Lee, Yeol Gyun Lee, Sung Ho Yun, Edmond Changkyun Park, Yeonhee Hong, Gun-Hwa Kim, Jae-Eun Park, Sun Jong Baek, Hyun Sik Kim, Seung Il Kim Journal of Microbiology.2013; 51(5): 659. CrossRef - Reevaluation of the Harboe Assay as a Standardized Method of Assessment for the Hemolytic Performance of Ventricular Assist Devices
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- Proteomic Analysis of Outer Membrane Proteins from Acinetobacter baumannii DU202 in Tetracycline Stress Condition
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Sung-Ho Yun , Chi-Won Choi , Soon-Ho Park , Je Chul Lee , Sun-Hee Leem , Jong-Soon Choi , Soohyun Kim , Seung Il Kim
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J. Microbiol. 2008;46(6):720-727. Published online December 24, 2008
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DOI: https://doi.org/10.1007/s12275-008-0202-3
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834
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Abstract
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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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Acinetobacter baumannii
Increases Tolerance to Antibiotics in Response to Monovalent Cations
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- Cyanobacterial Hybrid Kinase Sll0043 Regulates Phototaxis by Suppressing Pilin and Twitching Motility Protein
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Bong-Jeong Shin , Jeehyun Oh , Sungsoo Kang , Young-Ho Chung , Young Mok Park , Young Hwan Kim , Seungil Kim , Jong Bhak , Jong-Soon Choi
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J. Microbiol. 2008;46(3):300-308. Published online July 5, 2008
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DOI: https://doi.org/10.1007/s12275-007-0212-6
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692
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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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Citations
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Jong-Soon Choi, Yun Hwan Park, Soo Hyeon Kim, Ju Seong Park, Yoon-E Choi Environmental Biology Research.2020; 38(3): 424. CrossRef - Recent Advances in Biological Functions of Thick Pili in the Cyanobacterium Synechocystis sp. PCC 6803
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Klaus-Peter Michel, Ann-Kristin Schröder, Maike Zimmermann, Sonja Brandt, Elfriede K. Pistorius, Nicole Frankenberg-Dinkel, Dorothee Staiger Archives of Microbiology.2009; 191(6): 553. CrossRef - Transcriptional regulation of the cyanobacterial bidirectional Hox-hydrogenase
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- Cloning and Sequence Analysis of Two Catechol-degrading Gene Clusters from a Phenol-utilizing Bacterium Pseudomonas putida SM25
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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
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J. Microbiol. 2003;41(2):102-108.
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Abstract
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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.
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