A plastid enzyme arrested in the step of precursor translocation in vivo.
- Reinbothe S Institute for Plant Sciences, Department of Plant Genetics, Swiss Federal Institute of Technology Zurich, Zurich, Switzerland.
- Reinbothe C
- Neumann D
- Apel K
- 1996-10-15
Published in:
- Proceedings of the National Academy of Sciences of the United States of America. - 1996
English
The key enzyme of chlorophyll biosynthesis in higher plants, NADPH:protochlorophyllide (Pchlide) oxidoreductase (POR, EC 1.3.1.33), accumulates in its precursor form (pPORA) in barley. pPORA is bound to the chloroplasts and is able to interact with the enzyme's substrate, Pchlide, at both the cytosolic as well as the stromal side of the plastid envelope. The interaction with intraplastidic Pchlide, formed in ATP-containing chloroplasts upon feeding with -aminolevulinic acid, drives vectorial translocation of pPORA across the plastid envelope membranes. In contrast, exogenously applied Pchlide causes the release of the envelope-bound precursor protein to the cytosol. Both processes compete with each other if intra- and extraplastidic Pchlide are applied simultaneously. A cytosolic heat shock cognate protein of Mr 70,000 present in wheat germ and barley leaf protein extracts appears to prevent the release of the pPORA to the cytosol in vivo, however.
- Language
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- English
- Open access status
- bronze
- Identifiers
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- DOI 10.1073/pnas.93.21.12026
- PMID 11607713
- Persistent URL
- https://sonar.ch/global/documents/66969
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