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Human Molecular Genetics, 2001, Vol. 10, No. 3 259-269
© 2001 Oxford University Press

Distinct roles for two N-terminal cleaved domains in mitochondrial import of the yeast frataxin homolog, Yfh1p

Donna M. Gordon1, Mikhail Kogan2, Simon A.B. Knight2, Andrew Dancis2 and Debkumar Pain1,+

1Department of Physiology, University of Pennsylvania School of Medicine, D403 Richards Building, 3700 Hamilton Walk, Philadelphia, PA 19104-6085, USA and 2Department of Medicine, University of Pennsylvania School of Medicine, Philadelphia, PA 19104-6100, USA

The yeast frataxin homolog (Yfh1p) participates in mitochondrial iron homeostasis. The phenotypic defects of the {Delta}yfh1 mutant include drastic accumulation of iron in mitochondria and slow growth. The Yfh1p precursor protein contains two N-terminal domains that are sequentially cleaved by the matrix processing peptidase on import into mitochondria, generating the mature protein. We have precisely mapped these two cleavage sites. Mutations blocking the first or the second cleavage of Yfh1p do not interfere with its in vitro import or with its ability to complement phenotypes of the {Delta}yfh1 mutant strain. Distinct roles have been ascertained for the two cleaved domains of Yfh1p. The first cleaved domain (domain I) is sufficient for in vitro mitochondrial import of a non-mitochondrial passenger protein. However, neither domain I nor other matrix-targeting signals alone can support efficient in vitro import of mature Yfh1p. The second cleaved domain (domain II) is required as a spacer between a targeting signal and mature Yfh1p. Likewise, when Yfh1p constructs lacking domain I or II are expressed in vivo, they fail to attain appreciable steady-state amounts in mitochondria and cannot complement phenotypes of the {Delta}yfh1 mutant.

+ To whom correspondence should be addressed. Tel: +1 215 573 7305; Fax: +1 215 573 5851; Email: pain@mail.med.upenn.edu


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