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NADPH:Protochlorophyllide Oxidoreductase Uses the General Import Route into Chloroplasts
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Henrik Aronsson
Published/Copyright:
June 1, 2005
Abstract
Chloroplast differentiation in angiosperm plants depends on the light-dependent conversion of protochlorophyllide to chlorophyllide by NADPH:protochlorophyllide oxidoreductase (PORA; EC 1.6.99.1), a nuclearly encoded protein. The protein import of the precursor form of PORA into plastids was shown previously to strictly depend on the presence of its substrate protochlorophyllide. PORA seemed to follow a novel, posttranslationally regulated import route. Here we demonstrate that the precursor of PORA from barley is imported into isolated barley plastids independently of protochlorophyllide. PORA as well as PORB import is competed for by the precursor of the small subunit of Rubisco. The data demonstrate that the PORA precursor uses the general import pathway into plastids. Furthermore, en route into chloroplasts the pea POR precursor can be crosslinked to the protein import channel in the outer envelope Toc75 from pea.
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Published Online: 2005-06-01
Published in Print: 2000-12-18
Copyright © 2000 by Walter de Gruyter GmbH & Co. KG
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- Content Index
- Author Index
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Articles in the same Issue
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- Mannosidase Action, Independent of Glucose Trimming, Is Essential for Proteasome-Mediated Degradation of Unassembled Glycosylated Ig Light Chains
- Characterization of a Receptor for Heat Shock Protein 70 on Macrophages and Monocytes
- Yeast Translational Activator Cbs2p: Mitochondrial Targeting and Effect of Overexpression
- Mutational Scanning of a Hairpin Loop in the Tryptophan Synthase β-Subunit Implicated in Allostery and Substrate Channeling
- The Difference in the Carboxy-Terminal Sequence Is Responsible for the Difference in the Activity of Chicken and Rat Liver Fructose-2,6-Bisphosphatase
- Crystal Structure of the Caspase Activator Human Granzyme B, a Proteinase Highly Specific for an Asp-P1 Residue
- Primary Structure of Potato Kunitz-Type Serine Proteinase Inhibitor
- Activation of proPHBSP, the Zymogen of a Plasma Hyaluronan Binding Serine Protease, by an Intermolecular Autocatalytic Mechanism
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- Content Index
- Author Index
- Subject Index
