Johnson, N and Khan, A and Virji, S and Ward, JM and Crompton, M (1999) Import and processing of heart mitochondrial cyclophilin D. EUR J BIOCHEM , 263 (2) 353 - 359.
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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-35]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.
|Title:||Import and processing of heart mitochondrial cyclophilin D|
|Keywords:||cyclophilins, import, mitochondria, polymerase chain reaction, PERMEABILITY TRANSITION PORE, INNER MEMBRANE PORE, A-BINDING PROTEIN, CYCLOSPORINE-A, MULTIGENE FAMILY, INVOLVEMENT, ISOMERASES, CLEAVAGE, CLONING, CDNA|
|UCL classification:||UCL > School of Life and Medical Sciences > Faculty of Life Sciences > Biosciences (Division of)|
UCL > School of BEAMS > Faculty of Engineering Science > Biochemical Engineering
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