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A short C-terminal tail prevents mis-targeting of hydrophobic mitochondrial membrane proteins to the ER
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Seoul National University.
Seoul National University.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
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2013 (English)In: FEBS Letters, ISSN 0014-5793, E-ISSN 1873-3468, Vol. 587, no 21, 3480-6 p.Article in journal (Refereed) Published
Abstract [en]

Sdh3/Shh3, a subunit of mitochondrial succinate dehydrogenase, contains transmembrane domains with a hydrophobicity comparable to that of endoplasmic reticulum (ER) proteins. Here, we show that a C-terminal reporter fusion to Sdh3/Shh3 results in partial mis-targeting of the protein to the ER. This mis-targeting is mediated by the signal recognition particle (SRP) and depends on the length of the C-terminal tail. These results imply that if nuclear-encoded mitochondrial proteins contain strongly hydrophobic transmembrane domains and a long C-terminal tail, they have the potential to be recognized by SRP and mis-targeted to the ER.

Place, publisher, year, edition, pages
2013. Vol. 587, no 21, 3480-6 p.
Keyword [en]
Endoplasmic reticulum, mitochondria, signal sequence, co-translational translocation, succinate dehydrogenase
National Category
Biochemistry and Molecular Biology Cell Biology
Research subject
Biochemistry; Molecular Biology
Identifiers
URN: urn:nbn:se:su:diva-95375DOI: 10.1016/j.febslet.2013.08.041ISI: 000325978700018PubMedID: 24055247OAI: oai:DiVA.org:su-95375DiVA: diva2:661243
Note

AuthorCount: 6;

Funding agencies:

National Research Foundation of Korea 2012-0001935, C00048 

Available from: 2013-11-01 Created: 2013-10-26 Last updated: 2017-12-06Bibliographically approved
In thesis
1. Membrane Protein Biogenesis in Saccharomyces cerevisiae
Open this publication in new window or tab >>Membrane Protein Biogenesis in Saccharomyces cerevisiae
2013 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

Membranes are hydrophobic barriers that define the outer boundaries and internal compartments of living cells. Membrane proteins are the gates in these barriers, and they perform vital functions in the highly regulated transport of matter and information across membranes. Membrane proteins destined for the endoplasmic reticulum are targeted either co- or post-translationally to the Sec61 translocon, the major translocation machinery in eukaryotic cells, which allows for lateral partitioning of hydrophobic segments into the lipid bilayer. This thesis aims to acquire insights into the mechanism of membrane protein insertion and the role of different translocon components in targeting, insertion and topogenesis, using the yeast Saccharomyces cerevisiae as a model organism.

By measuring the insertion efficiency of a set of model proteins, we studied the sequence requirements for Sec61-mediated insertion of an α-helical transmembrane segment and established a ‘biological hydrophobicity scale’ in yeast, which describes the individual contributions of the 20 amino acids to insertion. Systematic mutagenesis and photo-crosslinking of the Sec61 translocon revealed key residues in the lateral gate that modulate the threshold hydrophobicity for membrane insertion and transmembrane segment orientation. Further, my studies demonstrate that the translocon-associated Sec62 is important not only for post-translational targeting, but also for the insertion and topogenesis of moderately hydrophobic signal anchor proteins and the C-terminal translocation of multi-spanning membrane proteins. Finally, nuclearly encoded mitochondrial membrane proteins were found to evade mis-targeting to the endoplasmic reticulum by containing short C-terminal tails.

Place, publisher, year, edition, pages
Stockholm: Department of Biochemistry and Biophysics, Stockholm University, 2013. 72 p.
National Category
Biochemistry and Molecular Biology
Research subject
Biochemistry
Identifiers
urn:nbn:se:su:diva-95376 (URN)978-91-7447-798-6 (ISBN)
Public defence
2013-12-13, Nordenskiöld Lecture Hall, Geo-Science Building, Svante Arrhenius väg 12, Stockholm, 13:00 (English)
Opponent
Supervisors
Note

At the time of the doctoral defence the following papers were unpublished and had a status as follows: Paper 4: Manuscript; Paper 5: Manuscript

Available from: 2013-11-21 Created: 2013-10-26 Last updated: 2014-07-25Bibliographically approved

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