Premium
Molecular chaperones and the biogenesis of mitochondria and peroxisomes
Author(s) -
Cuezva José M,
Flores Ana I,
Liras Antonio,
Santarén Juan F,
Alconada Agustín
Publication year - 1993
Publication title -
biology of the cell
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.543
H-Index - 85
eISSN - 1768-322X
pISSN - 0248-4900
DOI - 10.1016/s0248-4900(05)80174-1
Subject(s) - peroxisome , biology , protein targeting , chaperone (clinical) , mitochondrion , biogenesis , organelle , organelle biogenesis , microbiology and biotechnology , biochemistry , peroxisomal targeting signal , cytosol , membrane protein , gene , enzyme , medicine , pathology , membrane
Summary— A review of the proteinaceous machinery involved in protein sorting pathways and protein folding and assembly in mitochondria and peroxisomes is presented. After considering the various sorting pathways and targeting signals of mitochondrial and peroxisomal proteins, we make a comparative dissection of the protein factors involved in: i) the stabilization of cytosolic precursor proteins in a translocation competent conformation; ii) the membrane import apparatus of mitochondria and peroxisomes; iii) the processing of mitochondrial precursor proteins, and the eventual processing of certain peroxisomal precursor, in the interior of the organelles; and iv) the requirement of molecular chaperones for appropriate folding and assembly of imported proteins in the matrix of both organelles. Those aspects of mitochondrial biogenesis that have developed rapidly during the last few years, such as the requirement of molecular chaperones, are stressed in order to stimulate further parallel investigations aimed to understand the origin, biochemistry, molecular biology and pathology of peroxisomes. In this regard, a brief review of findings from our group and others is presented in which the role of the F 1 ‐ATPase α‐subunit is pointed out as a molecular chaperone of mitochondria and chloroplasts. In addition, data are presented that could question our previous indication that the immunoreactive protein found in the rat liver peroxisomes is due to the presence of the F 1 ‐ATPase α‐subunit.