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Heme incorporation into the cytochrome bo(3) occurs at a late stage of assembly
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
2012 (English)In: FEBS Letters, ISSN 0014-5793, E-ISSN 1873-3468, Vol. 586, no 23, 4197-4202 p.Article in journal (Refereed) Published
Abstract [en]

Respiratory complexes in both prokaryotes and eukaryotes contain multiple co-factors, which are coordinated in defined positions so that they can function as electron wires. Intriguingly, co-factors are usually buried deep within hetero-oligomeric protein complexes and it is not clear when or how they are incorporated. In this study we show that heme is incorporated into the cytochrome bo(3) complex of Escherichia coli at a late stage of assembly. Specifically the apo-form of subunit I (the catalytic subunit) interacts with subunits III and IV before accepting heme. Assembly of subunit II is stalled until heme is incorporated.

Place, publisher, year, edition, pages
2012. Vol. 586, no 23, 4197-4202 p.
Keyword [en]
Respiratory complex, Membrane protein assembly, Co-factor insertion, Heme, BN-PAGE, Escherichia coli inner membrane
National Category
Biochemistry and Molecular Biology
Research subject
Biochemistry
Identifiers
URN: urn:nbn:se:su:diva-84797DOI: 10.1016/j.febslet.2012.10.021ISI: 000311346100022OAI: oai:DiVA.org:su-84797DiVA: diva2:581579
Note

AuthorCount:2;

Available from: 2013-01-02 Created: 2013-01-02 Last updated: 2017-12-06Bibliographically approved
In thesis
1. The social life of a membrane protein; It's complex
Open this publication in new window or tab >>The social life of a membrane protein; It's complex
2013 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

Membrane proteins are key players in many biological processes. Since most membrane proteins are assembled into oligomeric complexes it is important to understand how they interact with each other. Unfortunately however, the assembly process (i.e. their social life) remains poorly understood. In the work presented in this thesis I have investigated when and how membrane proteins assemble with each other and their cofactors to form functional units. We have shown that that cofactor insertion in the hetero-tetrameric cytochrome bo3 occurs at an early state in the assembly process. We also found that the pentameric CorA magnesium ion channel is stabilised by different interactions depending on the magnesium ion concentration in the cell. These studies indicate that the assembly of a functional unit is a dynamic process, which is a result of many different forces. By studying the assembly of membrane proteins we have obtained a deeper insight into their function, which cannot be explained by static crystal structures.

Place, publisher, year, edition, pages
Stockholm: Department of Biochemistry and Biophysics, Stockholm University, 2013. 52 p.
Keyword
membrane proteins, assembly, cofactors, magnesium, Escherichia coli
National Category
Biochemistry and Molecular Biology
Research subject
Biochemistry
Identifiers
urn:nbn:se:su:diva-88597 (URN)978-91-7447-671-2 (ISBN)
Public defence
2013-05-03, Magnélisalen, Kemiska övningslaboratoriet, Svante Arrhenius väg 16 B, Stockholm, 10:00 (English)
Opponent
Supervisors
Note

At the time of the doctoral defense, the following paper was unpublished and had a status as follows: Paper 2: Manuscript.

Available from: 2013-04-11 Created: 2013-03-21 Last updated: 2013-03-29Bibliographically approved

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