A short C-terminal tail prevents mis-targeting of hydrophobic mitochondrial membrane proteins to the ER
2013 (English)In: FEBS Letters, ISSN 0014-5793, E-ISSN 1873-3468, Vol. 587, no 21, 3480-6 p.Article in journal (Refereed) Published
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.
Endoplasmic reticulum, mitochondria, signal sequence, co-translational translocation, succinate dehydrogenase
Biochemistry and Molecular Biology Cell Biology
Research subject Biochemistry; Molecular Biology
IdentifiersURN: urn:nbn:se:su:diva-95375DOI: 10.1016/j.febslet.2013.08.041ISI: 000325978700018PubMedID: 24055247OAI: oai:DiVA.org:su-95375DiVA: diva2:661243
National Research Foundation of Korea 2012-0001935, C00048 2013-11-012013-10-262013-12-02Bibliographically approved