The reducible complexity of a mitochondrial molecular machine


Por: Clements A., Bursac D., Gatsos X., Perry A.J., Civciristov S., Celik N., Likic V.A., Poggio S., Jacobs-Wagner C., Strugnell R.A., Lithgow T.

Publicada: 1 ene 2009
Categoría: Multidisciplinary

Resumen:
Molecular machines drive essential biological processes, with the component parts of these machines each contributing a partial function or structural element. Mitochondria are organelles of eukaryotic cells, and depend for their biogenesis on a set of molecular machines for protein transport. How these molecular machines evolved is a fundamental question. Mitochondria were derived from an ?-proteobacterial endosymbiont, and we identified in ?-proteobacteria the component parts of a mitochondrial protein transport machine. In bacteria, the components are found in the inner membrane, topologically equivalent to the mitochondrial proteins. Although the bacterial proteins function in simple assemblies, relatively little mutation would be required to convert them to function as a protein transport machine. This analysis of protein transport provides a blueprint for the evolution of cellular machinery in general.

Filiaciones:
Clements A.:
 Department of Biochemistry and Molecular Biology, Monash University, Clayton, VIC 3800, Australia

Bursac D.:
 Department of Biochemistry and Molecular Biology, Monash University, Clayton, VIC 3800, Australia

 Department of Biochemistry and Molecular Biology, University of Melbourne, Parkville, VIC 3010, Australia

Gatsos X.:
 Department of Biochemistry and Molecular Biology, University of Melbourne, Parkville, VIC 3010, Australia

Perry A.J.:
 Department of Biochemistry and Molecular Biology, Monash University, Clayton, VIC 3800, Australia

Civciristov S.:
 Department of Biochemistry and Molecular Biology, Monash University, Clayton, VIC 3800, Australia

 Department of Biochemistry and Molecular Biology, University of Melbourne, Parkville, VIC 3010, Australia

Celik N.:
 Department of Biochemistry and Molecular Biology, Monash University, Clayton, VIC 3800, Australia

Likic V.A.:
 Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, VIC 3010, Australia

Poggio S.:
 Department of Molecular, Cellular and Developmental Biology, Yale University, New Haven, CT 06520, United States

Jacobs-Wagner C.:
 Department of Molecular, Cellular and Developmental Biology, Yale University, New Haven, CT 06520, United States

 Howard Hughes Medical Institute, New Haven, CT 06520, United States

Strugnell R.A.:
 Department of Microbiology and Immunology, University of Melbourne, Parkville, VIC 3010, Australia

Lithgow T.:
 Department of Biochemistry and Molecular Biology, Monash University, Clayton, VIC 3800, Australia
ISSN: 00278424
Editorial
NATL ACAD SCIENCES, 2101 CONSTITUTION AVE NW, WASHINGTON, DC 20418 USA, Estados Unidos America
Tipo de documento: Article
Volumen: 106 Número: 37
Páginas: 15791-15795
WOS Id: 000269806600052
ID de PubMed: 19717453
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