NDLI: Calcium Status of Yellow Lupin Symbiosomes as a Potential Regulator of Their Nitrogenase Activity: The Role of the Peribacteroid Membrane

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Russian Journal of Plant Physiology : Volume 48, Issue 2, March 2001

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Russian Journal of Plant Physiology : Volume 47

Calcium Status of Yellow Lupin Symbiosomes as a Potential Regulator of Their Nitrogenase Activity: The Role of the Peribacteroid Membrane

Content Provider	Springer Nature Link
Author	Andreev, I. M. Andreeva, I. N. Dubrovo, P. N. Krylova, V. V. Kozhariva, G. M. Izmailov, S. F.
Copyright Year	2001
Abstract	The capacity of symbiosomes from yellow lupin root nodules for active Ca$^{2+}$uptake and the sensitivity of their nitrogenase activity to a disturbance of the symbiotic Ca partition were investigated. The experiments carried out on the isolated symbiosomes and the peribacteroid membrane (PBM) vesicles, using Ca$^{2+}$indicators arsenazo III and chlorotetracycline, and the cytochemical Ca visualization with potassium pyroantimonate (PA) provided evidence that an Mg-ATP-energized pump, most likely Mg$^{2+}$-dependent Ca$^{2+}$-ATPase catalyzing the active transport of Ca$^{2+}$from the cytosol of the plant cell into the symbiosomes across the PBM, functions on this membrane. Depleting the symbiosomes of Ca both in vivoandin vitroby treating the intact nodules of yellow lupin root or the purified symbiosomes isolated from the latter with EGTA and Ca$^{2+}$-ionophore A23187 substantially decreased their nitrogenase activity. The inhibitory effect of calcium deficit in the symbiosomes was not reversed by the addition of calcium to the incubation medium containing the plant tissues under study and was even enhanced under these conditions. The nitrogenase activity of the isolated symbiosomes not experiencing calcium deficit was also inhibited by the addition of relatively high concentrations of exogenous calcium to the incubation medium. These results seem to give evidence that the calcium status of nodule symbiosomes from yellow lupin roots controls their nitrogenase activity. The data obtained suggest that both Ca$^{2+}$transport on PBM and the low passive permeability of this membrane for the given cation play the key role in such a control.
Starting Page	308
Ending Page	317
Page Count	10
File Format	PDF
ISSN	10214437
Journal	Russian Journal of Plant Physiology
Volume Number	48
Issue Number	3
e-ISSN	16083407
Language	English
Publisher	Kluwer Academic Publishers-Plenum Publishers
Publisher Date	2001-01-01
Publisher Place	New York
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Plant Sciences
Content Type	Text
Resource Type	Article
Subject	Plant Science

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