TAILIEUCHUNG - Báo cáo khoa học: Integral membrane proteins in the mitochondrial outer membrane of Saccharomyces cerevisiae

Mitochondria evolved from a bacterial endosymbiont ancestor in which the integral outer membrane proteins would have been b-barrel structured within the plane of the membrane. Initial proteomics on the outer mem-brane from yeast mitochondria suggest that while most of the protein components are integral in the membrane, most of these mitochondrial pro-teins behave as if they have a-helical transmembrane domains, rather than b-barrels. | ềFEBS Journal Integral membrane proteins in the mitochondrial outer membrane of Saccharomyces cerevisiae Lena Burri1 Katherine Vascotto1 2 Ian E. Gentle1 2 Nickie C. Chan1 2 Traude Beilharz1 David I. Stapleton2 Lynn Ramage3 and Trevor Lithgow1 2 1 Department of Biochemistry and Molecular Biology University of Melbourne Parkville Australia 2 Bio21 Molecular Science and Biotechnology Institute Parkville Australia 3 Biozentrum University of Basel Switzerland Keywords detergent phase mitochondria outer membrane transmembrane segments Correspondence T. Lithgow Department of Biochemistry and Molecular Biology University of Melbourne Parkville 3010 Australia Fax 61 39348 2251 Tel 61 38344 4131 E-mail Present address Hoffmann-La Roche Ltd. CH-4070 Basel Switzerland Received 30 October 2005 revised 29 January 2006 accepted 9 February 2006 doi Mitochondria evolved from a bacterial endosymbiont ancestor in which the integral outer membrane proteins would have been b-barrel structured within the plane of the membrane. Initial proteomics on the outer membrane from yeast mitochondria suggest that while most of the protein components are integral in the membrane most of these mitochondrial proteins behave as if they have a-helical transmembrane domains rather than b-barrels. These proteins are usually predicted to have a single a-helical transmembrane segment at either the N- or C-terminus however more complex topologies are also seen. We purified the novel outer membrane protein Om14 and show it is encoded in the gene YBR230c. Protein sequencing revealed an intron is spliced from the transcript and both transcription from the YBR230c gene and steady-state level of the Om14 protein is dramatically less in cells grown on glucose than in cells grown on nonfermenta-ble carbon sources. Hydropathy predictions together with data from limited protease digestion show three a-helical transmembrane segments in Om14. The a-helical .

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