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Protein complexes of the Escherichia coli cell envelope
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
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2005 (English)In: Journal of Biological Chemistry, ISSN 0021-9258, E-ISSN 1083-351X, Vol. 280, no 41, 34409-34419 p.Article in journal (Refereed) Published
Abstract [en]

Protein complexes are an intrinsic aspect of life in the membrane. Knowing which proteins are assembled in these complexes is therefore essential to understanding protein function(s). Unfortunately, recent high throughput protein interaction studies have failed to deliver any significant information on proteins embedded in the membrane, and many membrane protein complexes remain ill defined. In this study, we have optimized the blue native-PAGE technique for the study of membrane protein complexes in the inner and outer membranes of Escherichia coli. In combination with second dimension SDS-PAGE and mass spectrometry, we have been able to identify 43 distinct protein complexes. In addition to a number of well characterized complexes, we have identified known and orphan proteins in novel oligomeric states. For two orphan proteins, YhcB and YjdB, our findings enable a tentative functional assignment. We propose that YhcB is a hitherto unidentified additional subunit of the cytochrome bd oxidase and that YjdB, which co-localizes with the ZipA protein, is involved in cell division. Our reference two-dimensional blue native-SDS-polyacrylamide gels will facilitate future studies of the assembly and composition of E. coli membrane protein complexes during different growth conditions and in different mutant backgrounds.

Place, publisher, year, edition, pages
2005. Vol. 280, no 41, 34409-34419 p.
Keyword [en]
Blotting; Western, Cell Cycle Proteins/chemistry/*pharmacology, Cell Division, Cell Membrane/*metabolism, Cytochromes/metabolism, Dimerization, Electron Transport Chain Complex Proteins/metabolism, Electrophoresis; Gel; Two-Dimensional, Electrophoresis; Polyacrylamide Gel, Escherichia coli/metabolism/*physiology, Escherichia coli Proteins/chemistry/metabolism/pharmacology/*physiology, Ions/chemistry, Macromolecular Substances/chemistry, Mass Spectrometry, Membrane Proteins/chemistry, Mutation, Oxidoreductases/chemistry/metabolism/*pharmacology, Protein Binding, Spectrometry; Mass; Matrix-Assisted Laser Desorption-Ionization
National Category
Biochemistry and Molecular Biology
Research subject
Biogeochemistry
Identifiers
URN: urn:nbn:se:su:diva-18892DOI: 10.1074/jbc.M506479200PubMedID: 16079137OAI: oai:DiVA.org:su-18892DiVA: diva2:185415
Available from: 2007-12-27 Created: 2007-12-27 Last updated: 2017-12-13Bibliographically approved
In thesis
1. Protein complexes of the Escherichia coli cell envelope
Open this publication in new window or tab >>Protein complexes of the Escherichia coli cell envelope
2010 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

The cell envelope of Escherichia coli, as for all living cells, is a magnificent semi-permeable membrane barrier that facilitates protection as well as enables fundamental contact with the exterior world. The envelope comprises a mixture of phospholipids, organized in two bilayers, which are stabilized by a rigid peptidoglycan layer. There are also a large number of proteins, which can be lipid-integrated or attached. Infact, it is anticipated that approximately 30-40% of the cellular proteome of E. coli could be associated with the envelope. These proteins are involved in the transport of small molecules and nutrients, the biogenesis of the envelope, metabolism, signaling, channeling and cellular movement and attachment.

The focus of this thesis is to understand the cell envelope of E. coli by understanding the proteins it holds. Three main questions have been addressed: 1) Which proteins are present? 2) How do these proteins interact? 3) How are the interactions brought about? To answer these questions we have designed and optimized methods suitable for proteome-wide separation, visualization and characterization of membrane proteins and protein complexes. We present reference proteome and interactome maps of the envelope, which further our understanding of the assembly and composition of the cell envelope. In many instances our studies have provided a first step towards understanding protein function(s) and for carrying out meaningful biochemical and structural analysis. We have also developed parallel approaches, which have enabled us to dissect the assembly process for two specific membrane protein complexes, a homo-dimer of penicillin binding protein 5 and the respiratory oxidase cytochrome bo3. These studies have extended our understanding of the relationship between structure and function of protein complexes.

Place, publisher, year, edition, pages
Stockholm: Department of Biochemistry and Biophysics, Stockholm University, 2010. 82 p.
National Category
Biochemistry and Molecular Biology
Research subject
Biochemistry
Identifiers
urn:nbn:se:su:diva-42248 (URN)978-91-7447-118-2 (ISBN)
Public defence
2010-10-11, Magnélisalen, Kemiska övningslaboratoriet, Svante Arrhenius väg 16 B, Stockholm, 14:00 (English)
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Note

At the time of the doctoral defense, the following papers were unpublished and had a status as follows: Paper 2: Submitted. Paper 4: Manuscript. Paper 5: Manuscript.

Available from: 2010-09-20 Created: 2010-08-19 Last updated: 2014-08-01Bibliographically approved

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