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Biogenesis of MalF and the MalFGK2 maltose transport complex in Escherichia coli requires YidC
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
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2008 (English)In: Journal of Biological Chemistry, ISSN 0021-9258, E-ISSN 1083-351X, no 283, 17881-17890 p.Article in journal (Refereed) Published
Abstract [en]

The polytopic inner membrane protein MalF is a constituent of the MalFGK2 maltose transport complex in Escherichia coli. We have studied the biogenesis of MalF using a combination of in vivo and in vitro approaches. MalF is targeted via the SRP pathway to the Sec/YidC insertion site. Despite close proximity of nascent MalF to YidC during insertion, YidC is not required for the insertion of MalF into the membrane. However, YidC is required for the stability of MalF and the formation of the MalFGK2 maltose transport complex. Our data indicate that YidC supports the folding of MalF into a stable conformation before it is incorporated into the maltose transport complex.

Place, publisher, year, edition, pages
2008. no 283, 17881-17890 p.
Keyword [en]
Membrane Transport, Structure, Function, and Biogenesis
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:su:diva-24886DOI: 10.1074/jbc.M801481200OAI: oai:DiVA.org:su-24886DiVA: diva2:198471
Available from: 2008-04-30 Created: 2008-04-30 Last updated: 2017-12-13Bibliographically approved
In thesis
1. From Biogenesis to Overexpression of Membrane Proteins in Escherichia coli
Open this publication in new window or tab >>From Biogenesis to Overexpression of Membrane Proteins in Escherichia coli
2008 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

In both pro- and eukaryotes 20-30% of all genes encode alpha-helical transmembrane domain proteins, which act in various and often essential capacities. Notably, membrane proteins play key roles in disease and they constitute more than half of all known drug targets.

The natural abundance of membrane proteins is in general too low to conveniently isolate sufficient material for functional and structural studies. Therefore, most membrane proteins have to be obtained through overexpression. Escherichia coli is one of the most successful hosts for overexpression of recombinant proteins. While the production of soluble proteins is comparably straightforward, overexpression of membrane proteins remains a challenging task. The yield of membrane localized recombinant membrane protein is usually low and inclusion body formation is a serious problem. Furthermore, membrane protein overexpression is often toxic to the host cell. Although several reasons can be postulated, the basis of these difficulties is not completely understood, preventing the design of rational strategies to improve membrane protein overexpression yields.

The objective of my Ph.D. studies has been to improve membrane protein overexpression in E. coli by a) understanding membrane protein overexpression from the perspective of membrane protein biogenesis, b) systematically investigating the physiological response to overexpression of membrane proteins and c) engineering strains that are optimized for membrane protein overexpression based on insights resulting from these studies.

By working toward these objectives, I was able to identify and alleviate one of the major bottlenecks of membrane protein overexpression in E. coli: saturation of the Sec-translocon could be overcome by harmonizing translation and membrane insertion of the recombinant membrane protein. This minimized the toxic effects of overexpression and thus resulted in increased membrane protein-producing biomass.

Place, publisher, year, edition, pages
Stockholm: Institutionen för biokemi och biofysik, 2008. 91 p.
National Category
Biochemistry and Molecular Biology
Research subject
Biochemistry
Identifiers
urn:nbn:se:su:diva-7513 (URN)978-91-7155-594-6 (ISBN)
Public defence
2008-05-23, Magnélisalen, Kemiska övningslaboratoriet, Svante Arrhenius väg 12 A, Stockholm, 10:00 (English)
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Available from: 2008-04-30 Created: 2008-04-30 Last updated: 2010-01-13Bibliographically approved

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