Translocation of mitochondrial inner-membrane proteins: conformation matters

de Marcos-Lousa, C., P Sideris, D. and Tokatlidis, K. (2006) Translocation of mitochondrial inner-membrane proteins: conformation matters. Trends in Biochemical Sciences, 31(5), pp. 259-267. (doi:10.1016/j.tibs.2006.03.006)

Full text not currently available from Enlighten.


Most of the mitochondrial inner-membrane proteins are generated without a presequence and their targeting depends on inadequately defined internal segments. Despite the numerous components of the import machinery identified by proteomics, the properties of hydrophobic import substrates remain poorly understood. Recent studies support several principles for these membrane proteins: first, they become organized into partially assembled forms within the translocon; second, they present noncontiguous targeting signals; and third, they induce conformational changes in translocase subunits, thereby mediating ‘assembly on demand’ of the import machinery. It is possible that the energy needed for these proteins to pass across the outer membrane, to travel through the intermembrane space and to target the inner-membrane surface is provided by conformational changes involving import components that seem to have natively unfolded structures. Such structural malleability might render some of the translocase subunits more adept at driving the protein import process.

Item Type:Articles
Glasgow Author(s) Enlighten ID:Tokatlidis, Professor Kostas
Authors: de Marcos-Lousa, C., P Sideris, D., and Tokatlidis, K.
College/School:College of Medical Veterinary and Life Sciences > Institute of Molecular Cell and Systems Biology
Journal Name:Trends in Biochemical Sciences

University Staff: Request a correction | Enlighten Editors: Update this record