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Signals Required for the Import and Processing of the Alternative Oxidase into Mitochondria
1999 (English)In: Journal of Biological Chemistry, ISSN 0021-9258, E-ISSN 1083-351X, Vol. 274, 1286-1293 p.Article in journal (Refereed) Published
Abstract [en]

The critical residues involved in targeting and processing of the soybean alternative oxidase to plant and animal mitochondria was investigated. Import of various site-directed mutants into soybean mitochondria indicated that positive residues throughout the length of the presequence were important for import, not just those in the predicted region of amphiphilicity. The position of the positive residues in the C-terminal end of the presequence was also important for import. Processing assays of the various constructs with purified spinach mitochondrial processing peptidase showed that all the −2-position mutants had a drastic effect on processing. In contrast to the import assay, the position of the positive residue could be changed for processing. Deletion mutants confirmed the site-directed mutagenesis data in that an amphiphilic α-helix was not the only determinant of mitochondrial import in this homologous plant system. Import of these constructs into rat liver mitochondria indicated that the degree of inhibition differed and that the predicted region of amphiphilic α-helix was more important with rat liver mitochondria. Processing with a rat liver matrix fraction showed little inhibition. These results are discussed with respect to targeting specificity in plant cells and highlight the need to carry out homologous studies and define the targeting requirements to plant mitochondria.

Place, publisher, year, edition, pages
1999. Vol. 274, 1286-1293 p.
Keyword [en]
PRE-ORNITHINE TRANSCARBAMYLASE; LIVER ALDEHYDE DEHYDROGENASE; PROTEIN IMPORT; TARGETING PEPTIDES; PRECURSOR PROTEINS; PLANT-MITOCHONDRIA; CYTOSOLIC FACTORS; CLEAVAGE SITES; LEADER PEPTIDE; BC(1) COMPLEX
National Category
Natural Sciences
Identifiers
URN: urn:nbn:se:sh:diva-8745DOI: 10.1074/jbc.274.3.1286ISI: 000079956900017OAI: oai:DiVA.org:sh-8745DiVA: diva2:420214
Available from: 2011-05-31 Created: 2011-05-31 Last updated: 2016-10-07Bibliographically approved

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CiteExportLink to record
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Cite
Citation style
  • apa
  • ieee
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  • vancouver
  • Other style
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  • de-DE
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