The targeting information of the mitochondrial outer membrane isoform of cytochrome b5 is contained within the carboxyl‐terminal region

FEBS Letters

De Silvestris, Marcella¹  D'Arrigo, Antonello¹  Borgese, Nica² 

[1] C.N.R. Center for Cytopharmacology, via Vanvitelli 32, 20129 Milano, Italy;Faculty of Pharmacy, University of Reggio, Calabria, Italy

关键词: Endoplasmic Reticulum;    Cytochrome b5;    Membrane biogenesis;    Membrane protein;    Mitochondrial outer membrane;    Protein targeting;    cyt;    cytochrome;    ER;    endoplasmic reticulum;    ER b 5;    endoplasmic reticulum isoform of cytochrome b 5;    NER-COM;    chimera between N-terminal domain of ER b 5 and C-terminal domain of OM b 5;    OM b 5;    outer mitochondrial membrane isoform of cytochrome b 5;    PDI;    protein disulphide isomerase;   

DOI  :  10.1016/0014-5793(95)00797-D

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Two isoforms of mammalian cytochrome b ₅, which have homologous cytosolic amino-terminal catalytic domains, are located one on endoplasmic reticulum (ER b ₅) the other on mitochondrial outer membranes (OM b ₅). A cDNA coding for the previously unknown carboxyl-terminal domain of OM b ₅ was cloned and a chimera between the catalytic domain of ER b ₅ and the carboxyl-terminal region of OM b ₅ was expressed in cultured mammlian cells. The chimera localized to mitochondria, indicating that the carboxyl-terminal 43 amino acids of OM b5 contain sufficient information to target the catalytic domain of ER b ₅ to the mitochondrial outer membrane.

【 授权许可】

Unknown