- 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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Abstract
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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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Citations
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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
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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
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- Isolation and Taxonomic Characterization of a Novel Type I Methanotrophic Bacterium
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Hee Gon Kim , Gui Hwan Han , Chi-Yong Eom , Si Wouk Kim
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J. Microbiol. 2008;46(1):45-50.
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DOI: https://doi.org/10.1007/s12275-008-0017-2
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721
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A methane-oxidizing bacterium was isolated from the effluent of manure and its molecular and biochemical properties were characterized. The isolate was aerobic, Gram-negative, and non-motile. The organism had a type I intracytoplasmic membrane structure and granular inclusion bodies. The outer cell wall surface (S-layers) was tightly packed with cup-shaped structures. Colonies were light yellow on nitrate mineral salt agar medium. In addition, the organism was catalase and oxidase positive. The isolate used the ribulose monophosphate (RuMP) pathway for carbon assimilation, and was able to utilize methane and methanol as a sole carbon and energy source, however, it could not utilize any other organic compounds that were tested. The cells grew well in a mixture of methane and air (methane:air=1:1, v/v) in a compulsory circulation diffusion system, and when grown under those conditions, the optimum pH was approximately 7.0 and the optimal temperature was 30°C. In addition, the specific growth rate and generation time were 0.13 per h and 5.43 h, respectively, when grown under the optimum conditions. The major ubiquinone was Q-8, and the G+C mol% of the DNA was 55.3. Phylogenetic analyses based on the 16S rRNA gene sequence comparisons showed that this bacterium belongs to a group of type I methanotrophs, and that it is most closely related to Methylomicrobium, with a sequence similarity of 99%. Therefore, the isolate was named Methylomicrobium sp. HG-1.
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