CDNA CLONING OF RAT MITOCHONDRIAL CYCLOPHILIN

Human cyclophilin-3 (hCyp-3) cDNA was used to screen a rat skeletal mu scle cDNA library which led to the isolation of a full-length cDNA enc oding the rat homologue. The derived amino acid sequence showed 89.5% identity with the human sequence, with major differences being restric ted to the mitochondrial targeting sequence. The N-terminal sequence o f the purified rat liver mitochondrial cyclophilin (CyP-D) corresponde d to that derived from the cDNA following 30 amino acids of targeting sequence. This confirms that hCyp-3 encodes mitochondrial matrix CyP ( CyP-D), which plays a crucial role in the mitochondrial permeability t ransition. CyP-D mRNA of a single sized (1.5 kb) was shown by Northern blotting to be present in liver, heart, skeletal muscle and brain. (C ) 1997 Elsevier Science B.V.