Article
- The EMBO Journal (2006) 25, 1603 - 1610
- doi:10.1038/sj.emboj.7601070
Published online: 6 April 2006
Subject Categories:
Mba1, a membrane-associated ribosome receptor in mitochondria
Martin Ott1, Martin Prestele1, Heike Bauerschmitt1, Soledad Funes1, Nathalie Bonnefoy2 and Johannes M Herrmann1
- Institut für Physiologische Chemie, Universität München, München, Germany
- Centre de Génétique Moléculaire du CNRS, Gif sur Yvette, France
Correspondence to:
Johannes M Herrmann, Institut für Physiologische Chemie, Universität München, Butenandtstrasse 5, München 81377, Germany. Tel.: +49 89 2180 77122; Fax: +49 89 2180 77093; E-mail: hannes.herrmann@med.uni-muenchen.de
Received 25 January 2006; Accepted 9 March 2006
Abstract
The genome of mitochondria encodes a small number of very hydrophobic polypeptides that are inserted into the inner membrane in a cotranslational reaction. The molecular process by which mitochondrial ribosomes are recruited to the membrane is poorly understood. Here, we show that the inner membrane protein Mba1 binds to the large subunit of mitochondrial ribosomes. It thereby cooperates with the C-terminal ribosome-binding domain of Oxa1, which is a central component of the insertion machinery of the inner membrane. In the absence of both Mba1 and the C-terminus of Oxa1, mitochondrial translation products fail to be properly inserted into the inner membrane and serve as substrates of the matrix chaperone Hsp70. We propose that Mba1 functions as a ribosome receptor that cooperates with Oxa1 in the positioning of the ribosome exit site to the insertion machinery of the inner membrane.
Keywords:
- Mba1,
- membrane insertion,
- mitochondria,
- Oxa1,
- protein synthesis
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