ArticlePlant molecular biology1997
Homologous and heterologous protein import into mitochondria isolated from the green alga Chlamydomonas reinhardtii.
Article in Plant molecular biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
4 citing papers in PubMed, 15 citations in OpenAlex.
- Reconstructing the mitochondrial protein import machinery of Chlamydomonas reinhardtii.Genetics · 2008Article
- Identification of novel mitochondrial protein components of Chlamydomonas reinhardtii. A proteomic approach.Plant physiology · 2003Article
- Structure, organization and expression of the genes encoding mitochondrial cytochrome c(1) and the Rieske iron-sulfur protein in Chlamydomonas reinhardtii.Molecular genetics and genomics : MGG · 2003Article
- Mitochondrial protein import in plants. Signals, sorting, targeting, processing and regulation.Plant molecular biology · 1998Review
Corrections and comments
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Authors and funding
5 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have established a homologous system for studying mitochondrial protein import in Chlamydomonas reinhardtii, using C. reinhardtii precursor proteins and mitochondria isolated from C. reinhardtii. The precursors of the F1 alpha ATP synthase subunit and the Rieske FeS protein were imported into mitochondria with high efficiency, while the F1 beta subunit precursor was imported with much lower efficiency. The import of heterologous precursor proteins from higher plants was also less efficient. The precursor of the C. reinhardtii PsaF chloroplast protein was converted into a protease-protected form upon incubation with mitochondria. In vitro processing studies revealed that in contrast to the situation in higher plants, the processing of the precursors was catalysed by a soluble, matrix-located peptidase.
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Registered trials
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