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PMID: 9428747 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Oxa1p mediates the export of the N- and C-termini of pCoxII from the mitochondrial matrix to the intermembrane space.

FEBS letters ·Vol. 418 ·No. 3 ·1997-12-01 ·Pages 367-70

Hell K, Herrmann J, Pratje E, Neupert W, Stuart RA

Abstract

Oxa1p is a mitochondrial protein reported to be involved in the assembly of the cytochrome oxidase complex. In the absence of a functional Oxa1p, subunit II of the cytochrome oxidase accumulates as its precursor form (pCoxII). Using mitochondria isolated from a yeast strain bearing a temperature sensitive mutation in the Oxa1p, pet ts1402, we have analyzed the function of the Oxa1p protein. We demonstrate that the accumulation of pCoxII in the pet ts1402 mitochondria does not reflect a compromised Imp1p activity in this mutant. Furthermore, measurement of the membrane potential has shown it to be sufficient to support the export of CoxII from the matrix. Rather, we found that newly synthesized pCoxII accumulates in the matrix of the pet ts1402 mitochondria, because export across the inner membrane is inhibited in the pet ts1402 mitochondria. In conclusion, Oxa1p mediates the export of the N- and C-termini of the mitochondrially encoded subunit II of cytochrome oxidase from the matrix to the intermembrane space.

MeSH Terms
Biological Transport Electron Transport Complex IV/genetics,metabolism Gene Expression Regulation, Fungal Mitochondria/metabolism Mitochondrial Proteins Nuclear Proteins/genetics,metabolism Peptides/metabolism Protein Precursors/genetics,metabolism Saccharomyces cerevisiae/metabolism,ultrastructure
Chemicals
Mitochondrial Proteins Nuclear Proteins OXA1 protein Peptides Protein Precursors mitochondrial addressing peptide Electron Transport Complex IV
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Hell K
Institut für Physiologische Chemie der Universität München, Munich, Germany.
Herrmann J
Pratje E
Neupert W
Stuart R A
Article Info
Journal
FEBS letters
Abbr.
FEBS Lett
ISSN
0014-5793
Published
1997-12-01
Pages
367-70
Language
English
Region
England
NLM ID
0155157
Subset
IM
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