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The human dynamin‐related protein OPA1 is anchored to the mitochondrial inner membrane facing the inter‐membrane space
Author(s) -
Olichon Aurélien,
Emorine Laurent J,
Descoins Eric,
Pelloquin Laetitia,
Brichese Laetitia,
Gas Nicole,
Guillou Emmanuelle,
Delettre Cécile,
Valette Annie,
Hamel Christian P,
Ducommun Bernard,
Lenaers Guy,
Belenguer Pascale
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)02985-x
Subject(s) - schizosaccharomyces pombe , dynamin , microbiology and biotechnology , biology , inner mitochondrial membrane , mitochondrion , inner membrane , mitochondrial carrier , mitochondrial dna , translocase of the inner membrane , saccharomyces cerevisiae , gene , genetics , bacterial outer membrane , mitochondrial membrane transport protein , cell , escherichia coli , endocytosis
Mutations in the OPA1 gene are associated with autosomal dominant optic atrophy. OPA1 encodes a dynamin‐related protein orthologous to Msp1 of Schizosaccharomyces pombe and Mgm1p of Saccharomyces cerevisiae , both involved in mitochondrial morphology and genome maintenance. We present immuno‐fluorescence and biochemical evidences showing that OPA1 resides in the mitochondria where it is imported through its highly basic amino‐terminal extension. Proteolysis experiments indicate that OPA1 is present in the inter‐membrane space and electron microscopy further localizes it close to the cristae. The strong association of OPA1 with membranes suggests its anchoring to the inner membrane.