Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
Why have Small Multidrug Resistance proteins not evolved into fused, internally homologous structures?
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Show others and affiliations
(English)Manuscript (preprint) (Other academic)
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:su:diva-94832OAI: oai:DiVA.org:su-94832DiVA: diva2:658717
Available from: 2013-10-22 Created: 2013-10-15 Last updated: 2013-10-25
In thesis
1. EmrE, a puzzling transporter: Assembly, biogenesis and evolution of a dual-topology membrane protein
Open this publication in new window or tab >>EmrE, a puzzling transporter: Assembly, biogenesis and evolution of a dual-topology membrane protein
2013 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

Biological membranes are the key to cell existence, as they are able to both isolate and connect their interior with the environment. Membranes are composed of lipids and proteins that create a semi-permeable barrier; because the lipid bilayer stops free diffusion of most molecules and ions, membrane proteins play an important role in connecting the interior of the cell with its environment. They function as receptors, sensing signals to trigger a response; cell adhesion molecules, holding neighboring cells together, or transporters and channels importing nutrients and extruding waste, among other chemical compounds, in a controlled manner.

In order for membrane proteins to function correctly, proper insertion, folding and oligomerization in the bilayer is essential. While most membrane proteins adopt a unique orientation in the membrane, some proteins adopt multiple topologies. A well-known case is the dual-topology membrane proteins that adopt two opposite orientations in the membrane. The best-studied dual-topology protein is EmrE, a dimeric multidrug transporter found in Escherichia coli, and other bacteria.

The existence of dual-topology proteins raises many questions regarding oligomerization, biogenesis and evolution of membrane proteins. In this thesis, EmrE has been used as a model protein to study some of these issues. Our goals were (i) to settle the controversy regarding whether the arrangement of the monomers within the EmrE dimer is parallel or antiparallel, (ii) to test the validity of the published X-ray structure by in vivo experiments and, (iii) to elucidate the mechanism of membrane insertion (iv) and the evolution of dual-topology membrane proteins.

Place, publisher, year, edition, pages
Stockholm: Department of Biochemistry and Biophysics, Stockholm University, 2013. 68 p.
National Category
Biochemistry and Molecular Biology
Research subject
Biochemistry
Identifiers
urn:nbn:se:su:diva-94830 (URN)978-91-7447-797-9 (ISBN)
Public defence
2013-12-06, Magnélisalen, Kemiska övningslaboratoriet, Svante Arrhenius väg 16 B, Stockholm, 10:00 (English)
Opponent
Supervisors
Note

At the time of the doctoral defence the following papers were unpublished and had a status as follows: Paper 2: Epub ahead of print; Paper 4: Manuscript

Available from: 2013-11-14 Created: 2013-10-15 Last updated: 2013-11-05Bibliographically approved

Open Access in DiVA

No full text

Search in DiVA

By author/editor
Lloris-Garcerá, PilarRapp, Mikaelavon Heijne, Gunnar
By organisation
Department of Biochemistry and Biophysics
Biochemistry and Molecular Biology

Search outside of DiVA

GoogleGoogle Scholar

urn-nbn

Altmetric score

urn-nbn
Total: 217 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf