Proteomic study of the peripheral proteins from thylakoid membranes of the cyanobacteriumSynechocystis sp. PCC 6803

Wang, Yingchun; Sun, Jun; Chitnis, Parag R.

doi:10.1002/(sici)1522-2683(20000501)21:9<1746::aid-elps1746>3.0.co;2-o

Cited by 66 publications

(17 citation statements)

References 22 publications

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“…The envelope membrane protein list compiled in this study was further compared to protein lists derived from other published chloroplastic or mitochondrial proteome studies. 10,[16][17][18]32,35 As expected, no envelope membrane proteins identified in this study were similarly detected in the mitochondrial proteome study. 32,35 However, several proteins identified in the thylakoid proteome projects of Peltier et al 10 and Schubert et al 17 were identified in our envelope proteome (see Table 2).…”

Section: Total Envelope Membrane Proteins Identified By Both Gel-c-mssupporting

confidence: 68%

“…53,54 Already, several chloroplastic proteome investigations have been completed. 10,17,18 More recently, a limited proteomic analysis of the integral membrane proteins of spinach envelopes has been accomplished. 20 Likewise, the proteome of another plastid type, the wheat amyloplast, has also been studied.…”

Section: Benefits Of Using Multiple Mass Spectrometry Techniquesmentioning

confidence: 99%

“…Already, several proteomic studies focusing on the thylakoids of the chloroplasts have been completed. 10,[16][17][18] The methods employed in these studies relied heavily on two-dimensional (2D) electrophoresis, followed by excision of protein spots from these gel systems and subsequent proteolytic digestion and identification of proteins by either matrix-assisted laser desorption ionization/ time-of-flight mass spectrometry (MALDI-TOF-MS) or by electrospray liquid chromatography coupled with tandem mass spectrometry (LC-MS/MS) analysis. However, with regard to the envelope membranes, only a small fraction of the proteins present have been identified and characterized.…”

Section: Introductionmentioning

confidence: 99%

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Proteomic Study of the Arabidopsis thaliana Chloroplastic Envelope Membrane Utilizing Alternatives to Traditional Two-Dimensional Electrophoresis

et al. 2003

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With the completion of the sequencing of the Arabidopsis genome and with the significant increase in the amount of other plant genome and expressed sequence tags (ESTs) data, plant proteomics is rapidly becoming a very active field. We have pursued a high-throughput mass spectrometry-based proteomics approach to identify and characterize membrane proteins localized to the Arabidopsis thaliana chloroplastic envelope membrane. In this study, chloroplasts were prepared from plate- or soil-grown Arabidopsis plants using a novel isolation procedure, and "mixed" envelopes were subsequently isolated using sucrose step gradients. We applied two alternative methodologies, off-line multidimensional protein identification technology (Off-line MUDPIT) and one-dimensional (1D) gel electrophoresis followed by proteolytic digestion and liquid chromatography coupled with tandem mass spectrometry (Gel-C-MS/MS), to identify envelope membrane proteins. This proteomic study enabled us to identify 392 nonredundant proteins.

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Section: Total Envelope Membrane Proteins Identified By Both Gel-c-mssupporting

confidence: 68%

Section: Benefits Of Using Multiple Mass Spectrometry Techniquesmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Proteomic Study of the Arabidopsis thaliana Chloroplastic Envelope Membrane Utilizing Alternatives to Traditional Two-Dimensional Electrophoresis

et al. 2003

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“…Transmembrane proteins are underrepresented on 2-D gels due to their extreme hydrophobicity [12]. The multiple chaotrope buffer used in this study is not effective in solubilizing intrinsic membrane proteins that have been precipitated using TCA [13]. Nevertheless, we found nine spots that were identified as the integral membrane proteins of the light-harvesting complexes of photosystem I (LHCI) and photosystem II (LHCII).…”

Section: Resolution and Identification Of The Proteins From Maize Leavesmentioning

confidence: 81%

The proteome of maize leaves: Use of gene sequences and expressed sequence tag data for identification of proteins with peptide mass fingerprints

Porubleva

Velden²,

Kothari³

et al. 2001

Electrophoresis

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As a first step in establishing a proteome database for maize, we have embarked on the identification of the leaf proteins resolved on two-dimensional (2-D) gels. We detected nearly 900 spots on the gels with a pH 4-7 gradient and over 200 spots on the gels with a pH 6-11 gradient when the proteins were visualized with colloidal Coomassie blue. Peptide mass fingerprints for 300 protein spots were obtained with matrix assisted laser desorption/ionization-time of flight (MALDI-TOF) mass spectrometer and 149 protein spots were identified using the protein databases. We also searched the pdbEST databases to identify the leaf proteins and verified 66% of the protein spots that had been identified using the protein databases. Sixty-seven additional protein spots were identified from expressed sequence tags (ESTs). Many abundant leaf proteins are present in multiple spots. Functions of over 50% of the abundant leaf proteins are either unknown or hypothetical. Our results show that EST databases in conjunction with peptide mass fingerprints can be used for identifying proteins from organisms with incomplete genome sequence information.

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“…Of these, 47 were not among the 143 independent gene products identified in Cyano 2D Base. A proteomic study on the peripheral proteins associated with the thylakoid membranes of Synechocystis PCC6803 resolved more than 200 proteins on 2-D gels [18]. From these, 116 were analysed by peptide mass fingerprinting and 78 proteins were identified which were derived from genes, 24 of which were not previously identified in CyanoBase.…”

Section: Introductionmentioning

confidence: 99%

Proteomic study of the soluble proteins from the unicellular cyanobacterium Synechocystis sp. PCC6803 using automated matrix-assisted laser desorption/ionization-time of flight peptide mass fingerprinting

et al. 2002

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The unicellular cyanobacteria Synechocystis sp. (PCC6803) has become a model organism for a range of biochemical and molecular biology studies aimed at investigating environmental stress responses. In this study the soluble proteins of Synechocystis were analysed using narrow pH range (pH 4.5-5.5) zoom gels, automated matrix-assisted laser desorption/ionization mass spectrometry acquisition, spectral processing and database searching. The work sets the foundation for investigations of proteomic changes following stress treatment. One hundred and ninety-two protein spots were analysed and 105 proteins identified, of these 37 were novel proteins not previously seen on two-dimensional gels. Proteins involved in amino acid biosynthesis, energy metabolism and protein modification were identified using this fully automated procedure demonstrating that automated acquisition and processing will be a useful tool for proteomic analyses on this organism.

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Proteomic study of the peripheral proteins from thylakoid membranes of the cyanobacteriumSynechocystis sp. PCC 6803

Cited by 66 publications

References 22 publications

Proteomic Study of the Arabidopsis thaliana Chloroplastic Envelope Membrane Utilizing Alternatives to Traditional Two-Dimensional Electrophoresis

Proteomic Study of the Arabidopsis thaliana Chloroplastic Envelope Membrane Utilizing Alternatives to Traditional Two-Dimensional Electrophoresis

The proteome of maize leaves: Use of gene sequences and expressed sequence tag data for identification of proteins with peptide mass fingerprints

Proteomic study of the soluble proteins from the unicellular cyanobacterium Synechocystis sp. PCC6803 using automated matrix-assisted laser desorption/ionization-time of flight peptide mass fingerprinting

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