ArticlePlant molecular biology2002
Chloroplast protein import inhibition by a soluble factor from wheat germ lysate.
Article in Plant molecular biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 25 citations in OpenAlex.
- Article
- Phosphorylation and Dephosphorylation of the Presequence of Precursor MULTIPLE ORGANELLAR RNA EDITING FACTOR3 during Import into Mitochondria from Arabidopsis.Plant physiology · 2015Article
- Functional definition of outer membrane proteins involved in preprotein import into mitochondria.The Plant cell · 2007Article
- Functional specialization amongst the Arabidopsis Toc159 family of chloroplast protein import receptors.The Plant cell · 2004Article
- Identification of signals required for import of the soybean F(A)d subunit of ATP synthase into mitochondria.Plant molecular biology · 2004Article
- Investigations on the in vitro import ability of mitochondrial precursor proteins synthesized in wheat germ transcription-translation extract.Plant molecular biology · 2003Article
- Characterization of the translocon of the outer envelope of chloroplasts.The Journal of cell biology · 2003Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein import into chloroplasts occurs post-translationally in vitro. The precursor proteins are generally synthesised in a reticulocyte lysate- or wheat germ lysate-derived system and imported out of this system into chloroplast. These complex soluble protein mixtures are likely to contain factors, which influence somehow the import competence and import efficiency. Here we describe a heat-stable soluble proteinaceaous factor, which inhibits protein import into chloroplasts in vitro. The inhibitor interacts directly with the precursor protein and renders it import incompetent. This mode of action is supported by two observations: firstly, binding of the precursor to the chloroplast surface is diminished in the presence of the inhibitor. Secondly, when chloroplasts were loaded with precursor proteins under conditions, which allow only binding but not import the inhibitor was unable to abolish the subsequent translocation step.
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Registered trials
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