The structure of outer mitochondrial protein import receptors
AuthorPerry, Andrew J.
AffiliationSchool of Medicine: Biochemistry and Molecular Biology
Biochemistry and Molecular Biology
Document TypePhD thesis
CitationsPerry, A. J. (2007). The structure of outer mitochondrial protein import receptors. PhD thesis, Biochemistry and Molecular Biology, University of Melbourne.
Access StatusOpen Access
© 2007 Andrew J. Perry.
Mitochondria evolved through endosymbiosis of an ancient prokaryote, and subsequently lost most genes to the host genome. In order for mitochondrial proteins to be correctly localized from the host cytosol to the mitochondrial compartments, a complex protein targeting and import machinery has evolved. Key receptor components in the protein translocase complex of the outer mitochondrial membrane, Tom20 and Tom22, recognize proteins to be imported and assist their insertion across the outer membrane. The solution structure of the Tom20 receptor domain from Arabidopsis thaliana was determined by nuclear magnetic resonance spectroscopy, and revealed that this protein has significant structural differences to its functional analogue found in animals and fungi.
Keywordsprotein structure; protein import; nuclear magnetic resonance; mitochondria; protein evolution
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