Journal Article

Maturation of Wild-Type and Mutated Frataxin by the Mitochondrial Processing Peptidase

Hana Koutnikova, Victoria Campuzano and Michel Koenig

in Human Molecular Genetics

Volume 7, issue 9, pages 1485-1489
Published in print September 1998 | ISSN: 0964-6906
Published online September 1998 | e-ISSN: 1460-2083 | DOI: http://dx.doi.org/10.1093/hmg/7.9.1485
Maturation of Wild-Type and Mutated Frataxin by the Mitochondrial Processing Peptidase

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Frataxin is a mitochondrial protein deficient in Friedreich ataxia (FRDA) and which is associated yeast two-hybrid assay. In in vitro assays, MPP|b binds frataxin which is cleaved by the reconstituted MPP heterodimer. MPP cleavage of fratwith abnormal intramitochondrial iron handling. We identified the mitochondrial processing peptidase β (MPPβ) as a frataxin protein partner using the axin results in an intermediate form (amino acids 41–210) that is processed further to the mature form. In vitro and in vivo experiments suggest that two C-terminal missense mutations found in FRDA patients modulate interaction with MPPβ, resulting in a slower maturation process at the normal cleavage site. The slower processing rate of frataxin carrying such missense mutations may therefore contribute to frataxin deficiency, in addition to an impairment of its function.

Journal Article.  3936 words.  Illustrated.

Subjects: Genetics and Genomics

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