Journal article

The transmembrane segment of Tom20 is recognized by Mim1 for docking to the mitochondrial TOM complex

Joanne M Hulett, Franziska Lueder, Nickie C Chan, Andrew J Perry, Peter Wolynec, Vladimir A Likic, Paul R Gooley, Trevor Lithgow

JOURNAL OF MOLECULAR BIOLOGY | ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD | Published : 2008

Abstract

Mitochondria cannot be made de novo. Mitochondrial biogenesis requires that up to 1000 proteins are imported into mitochondria, and the protein import pathway relies on hetero-oligomeric translocase complexes in both the inner and outer mitochondrial membranes. The translocase in the outer membrane, the TOM complex, is composed of a core complex formed from the beta-barrel channel Tom40 and additional subunits each with single, alpha-helical transmembrane segments. How alpha-helical transmembrane segments might be assembled onto a transmembrane beta-barrel in the context of a membrane environment is a question of fundamental importance. The master receptor subunit of the TOM complex, Tom20, ..

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University of Melbourne Researchers