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Import and processing of heart mitochondrial cyclophilin D

Johnson, N; Khan, A; Virji, S; Ward, JM; Crompton, M; (1999) Import and processing of heart mitochondrial cyclophilin D. European Journal of Biochemistry , 263 (2) 353 - 359. 10.1046/j.1432-1327.1999.00490.x.

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Abstract

Cyclophilins are a family of cyclosporin-A-binding proteins which catalyse rotation about prolyl peptide bonds. A mitochondrial isoform in mammalian cells, cyclophilin D, is a component of the permeability transition pore that is formed by the adenine nucleotide translocase and the voltage- dependent anion channel at contact sites between the inner and outer membrane. This study investigated the submitochondrial location of cyclophilin D by following the fate of radiolabelled protein following import. Precursor [S]cyclophilin D was expressed in vitro from a PCR- generated cDNA. The precursor was imported by rat heart mitochondria and processed in a single step to a 21-kDa protein that was identical (SDS/PAGE) to an in vitro expressed mature protein and a cyclophilin D purified from rat heart mitochondria. No further modification of the mature protein could be demonstrated. Fractionation of mitochondria following import established that cyclophilin D locates only to the matrix. It is concluded that cyclophilin D binding to the permeability transition pore must occur at the inner face of the mitochondrial inner membrane.

Type:Article
Title:Import and processing of heart mitochondrial cyclophilin D
DOI:10.1046/j.1432-1327.1999.00490.x
UCL classification:UCL > School of Life and Medical Sciences > Faculty of Life Sciences > Biosciences (Division of)

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