Characterization of the regulatory function of the 46-kDa isoform of Rubisco activase from Arabidopsis.
作者： Ning Zhang , Peter Schürmann , Archie R. Portis, Jr
关键词: Gene isoform 、 Fructose 、 Spinach 、 RuBisCO 、 Light intensity 、 Arabidopsis 、 Thioredoxin 、 Biochemistry 、 ATP hydrolysis 、 Biology 、 Molecular biology
摘要: Arabidopsis Rubisco activase was recently shown to be regulated by redox changes in the larger (46-kDa) isoform specifically mediated thioredoxin-f [Zhang and Portis (1999) Proc Natl Acad Sci USA 96: 9438–9443]. Reduction greatly increases activity of 46-kDa native protein at physiological ATP/ADP ratios. In this study we conducted additional experiments characterize regulation thioredoxin-f. The Km for both ATP hydrolysis activation lowered 4 5-fold after reduction, but maximum increased only 10%. Only 0.35 μM required a half-maximal change 10 min preincubation with 1 complete min. Equal amounts 43-kDa isoforms were inhibition reduction-oxidation cycle assay an ratio 3:1, whereas inhibited 50% 2:1 (43-/46-kDa) isoforms. This requirement is consistent fact that normally contains about 1:1 two mRNA levels. Redox titrations indicated midpoint potential −344 mV as compared −342 spinach fructose 1,6-bisphosphatase pH 7.9, previous reports indicating these proteins are co-regulated light intensity similar manner.
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