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Differential sublocalization of the dynamin-related protein OPA1 isoforms in mitochondria.

Abstract：

:OPA1 is a cause gene for autosomal dominant optic atrophy and possesses eight alternative splicing variants. Here, we identified two isoforms of OPA1 proteins in HeLa cells and examined their submitochondrial localization and complex formations. RT-PCR shows that HeLa cells mainly express isoforms 7 and 1 of OPA1. Since the third cleavage site is mainly utilized in HeLa cells, the predicted molecular masses of their processed proteins are consistent with the 93- and 88-kDa proteins. Biochemical examinations indicate that both of the OPA1 isoforms are present in the intermembrane space. Submitochondrial fractionation by sucrose density-gradient centrifugation shows that the 88-kDa protein predominantly associates with the mitochondrial outer membrane, on the contrary, the 93-kDa protein associates with the inner membrane. Gel filtration analysis indicates that they compose the different molecular mass complexes in mitochondria. These differences between two isoforms of OPA1 would suggest their crucial role involved in the mitochondrial membrane formation.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Satoh M,Hamamoto T,Seo N,Kagawa Y,Endo H

doi

10.1016/s0006-291x(02)02874-7

subject

Has Abstract

pub_date

2003-01-10 00:00:00

pages

482-93

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006291X02028747

journal_volume

300

pub_type

杂志文章

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