Characterization of nucleoside triphosphatase activity in isolated pea nuclei and its photoreversible regulation by light.

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 Mg(2+)-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.

journal_name

Plant Physiol

journal_title

Plant physiology

authors

Chen YR,Roux SJ

doi

10.1104/pp.81.2.609

subject

Has Abstract

pub_date

1986-01-01 00:00:00

pages

609-13

eissn

0032-0889

issn

1532-2548

journal_volume

81

pub_type

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