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. 1986 Jun;81(2):609–613. doi: 10.1104/pp.81.2.609

Characterization of Nucleoside Triphosphatase Activity in Isolated Pea Nuclei and Its Photoreversible Regulation by Light 1

Yuh-Ru Chen 1, Stanley J Roux 1
PMCID: PMC1075385  PMID: 11538660

Abstract

A nucleoside triphosphatase (NTPase) present in highly purified preparations of pea nuclei was partially characterized. The activity of this enzyme was stimulated by divalent cations (Mg2+ = Mn2+ > Ca2+), but was not affected by the monovalent cations, Na+ and K+. The Mg2+-dependent activity was further stimulated by concentrations of Ca2+ in the low micromolar range. It could catalyze the hydrolysis of ATP, GTP, UTP, and CTP, all with a pH optimum of 7.5. The nuclear NTPase activity was not inhibited by vanadate, oligomycin, or nitrate, but was inhibited by relatively low concentrations of quercetin and the calmodulin inhibitor, compound 48/80. The NTPase was stimulated more than 50% by red light, and this effect was reversed by subsequent irradiation with far-red light. The photoreversibility of the stimulation indicated that the photoreceptor for this response was phytochrome, an important regulator of photomorphogenesis and gene expression in plants.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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