A rapidly light‐induced chloroplast protein with a high turnover coded for by pea nuclear DNA
- 1 January 1984
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 138 (1) , 201-207
- https://doi.org/10.1111/j.1432-1033.1984.tb07900.x
Abstract
Among the translation products obtained in vitro with mRNA isolated from etiolated grown pea, or after different times of illumination following the etiolation, a 24,000 MW protein was observed in the very early phase of greening; its occurrence culminates at 2-4 h after the start of illumination. The corresponding mRNA appears in and disappears from the poly(A)-containing RNA population within hours. The protein product was characterized as the precursor for a 17,000 MW chloroplast protein; by means of post-translational transport in vitro, the processed product becomes bound to chloroplast membranes. A product of the same size can also be labeled in vivo with a maximum of incorporation of label at 6-8 h after illumination. This product decays with a half-life of about 5 h. These findings imply a regulatory function of the 17,000 MW protein during the process of greening, possibly by synchronization of nuclear and chloroplast genomes. Other possibilities are considered.This publication has 31 references indexed in Scilit:
- Purification of the Steroid-Binding Core of Porcine Estrogen ReceptorHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1983
- Transport of Proteins into ChloroplastsEuropean Journal of Biochemistry, 1982
- The Protochlorophyllide Holochrome of Barley (Hordeum Vulgare L.)European Journal of Biochemistry, 1981
- The Protochlorophyllide Holochrome of Barley (Hordeum vulgare L.)European Journal of Biochemistry, 1981
- Biosynthesis of the Light‐Harvesting Chlorophyll a/b ProteinEuropean Journal of Biochemistry, 1981
- Biosynthesis of the Light‐Harvesting Chlorophyll a/b ProteinEuropean Journal of Biochemistry, 1981
- Light Effects on the Synthesis of Ribulose-1,5-Bisphosphate Carboxylase in Lemna gibba L. G-3Plant Physiology, 1980
- Plastid Protease Activity and Prolamellar Body Transformation during GreeningPlant Physiology, 1980
- The chlorophyll‐protein complexes of the thylakoid in greening plastids of Phaseolus vulgarisFEBS Letters, 1979
- Phytochrome‐Induced Appearance of mRNA Activity for the Apoprotein of the Light‐Harvesting Chlorophyll a/b Protein of Barley (Hordeum vulgare)European Journal of Biochemistry, 1979