PMID:16858726: Difference between revisions

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<span style = 'font-size: large'> '''Lasserre, JP, Beyne, E, Pyndiah, S, Lapaillerie, D, Claverol, S and Bonneu, M'''  (2006) A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis.''Electrophoresis'' '''27''':3306-21</span>
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|{{TableHeadingColor}} |'''Abstract''' || Study of the complexome - all the protein complexes of the cell - is essential for a better understanding and more global vision of cell function. Using two-dimensional blue native/SDS-PAGE (2-D BN/SDS-PAGE) technology, the cytosolic and membrane protein complexes of Escherichia coli were separated. Then, the different partners of each protein complex were identified by LC-MS/MS. In this report, 306 protein complexes were separated and identified. Among these protein complexes, 50 heteromultimeric and 256 homomultimeric protein complexes were found. Among the 50 heteromultimeric protein complexes, 18 previously described protein complexes validate the technology. In this study, 109 new protein complexes were found, providing insight into the function of previously uncharacterized bacterial proteins.
!align=left  |Citation
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'''Lasserre, JP, Beyne, E, Pyndiah, S, Lapaillerie, D, Claverol, S and Bonneu, M'''  (2006) A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis. ''Electrophoresis'' '''27''':3306-21
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!align=left  |Abstract
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Study of the complexome - all the protein complexes of the cell - is essential for a better understanding and more global vision of cell function. Using two-dimensional blue native/SDS-PAGE (2-D BN/SDS-PAGE) technology, the cytosolic and membrane protein complexes of Escherichia coli were separated. Then, the different partners of each protein complex were identified by LC-MS/MS. In this report, 306 protein complexes were separated and identified. Among these protein complexes, 50 heteromultimeric and 256 homomultimeric protein complexes were found. Among the 50 heteromultimeric protein complexes, 18 previously described protein complexes validate the technology. In this study, 109 new protein complexes were found, providing insight into the function of previously uncharacterized bacterial proteins.
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!align=left  |Links
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=16858726 PubMed]
Online version:[http://dx.doi.org/10.1002/elps.200500912 10.1002/elps.200500912]
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|{{TableHeadingColor}} nowrap |'''Links''' ||  [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=16858726 PubMed]
!align=left  |Keywords
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Chromatography, Liquid; Electrophoresis, Gel, Two-Dimensional/methods; Electrophoresis, Polyacrylamide Gel/methods; Escherichia coli/chemistry; Escherichia coli/metabolism; Escherichia coli Proteins/analysis; Escherichia coli Proteins/classification; Escherichia coli Proteins/metabolism; Mass Spectrometry; Proteome/analysis; Proteome/metabolism
 
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==Significance {{HelpIcon|Help:Literature}} ==
==Significance {{HelpIcon|Help:Literature}} ==
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==Annotations {{HelpIcon|Help:Literature}}==
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!|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
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TpiA
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GO:0005737
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cytoplasm
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IDA: Inferred from Direct Assay
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C
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Supplemental information, row 163 of table.
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complete
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[[mscL:Gene_Product(s)|MscL]]
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GO:0005624
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membrane fraction
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IDA: Inferred from Direct Assay
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C
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complete
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YbbN
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GO:0005737
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cytoplasm
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IDA: Inferred from Direct Assay
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C
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Supplemental information.
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complete
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tdcE, 2-ketobutyrate formate-lyase/pyruvate formate-lyase 4, inactive
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GO:0005624
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membrane fraction
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IDA: Inferred from Direct Assay
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C
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Table 3. Unknown cytosolic and membrane homomultimeric complexes, tdcE is complex 299.
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complete
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AceF, the "E2" or "core" component of the pyruvate dehydrogenase multienzyme complex
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GO:0005737
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cytoplasm
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IDA: Inferred from Direct Assay
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C
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Table 1. Known cytosolic (C) and membrane (M) heteromultimeric protein complexes, complex 3.
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complete
 
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==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
==EcoliWiki Links {{HelpIcon|Help:Literature}} ==

Latest revision as of 04:30, 15 September 2013

Citation

Lasserre, JP, Beyne, E, Pyndiah, S, Lapaillerie, D, Claverol, S and Bonneu, M (2006) A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis. Electrophoresis 27:3306-21

Abstract

Study of the complexome - all the protein complexes of the cell - is essential for a better understanding and more global vision of cell function. Using two-dimensional blue native/SDS-PAGE (2-D BN/SDS-PAGE) technology, the cytosolic and membrane protein complexes of Escherichia coli were separated. Then, the different partners of each protein complex were identified by LC-MS/MS. In this report, 306 protein complexes were separated and identified. Among these protein complexes, 50 heteromultimeric and 256 homomultimeric protein complexes were found. Among the 50 heteromultimeric protein complexes, 18 previously described protein complexes validate the technology. In this study, 109 new protein complexes were found, providing insight into the function of previously uncharacterized bacterial proteins.

Links

PubMed Online version:10.1002/elps.200500912

Keywords

Chromatography, Liquid; Electrophoresis, Gel, Two-Dimensional/methods; Electrophoresis, Polyacrylamide Gel/methods; Escherichia coli/chemistry; Escherichia coli/metabolism; Escherichia coli Proteins/analysis; Escherichia coli Proteins/classification; Escherichia coli Proteins/metabolism; Mass Spectrometry; Proteome/analysis; Proteome/metabolism

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