H+‐translocating ATPase and Na+/H+ antiport activities in the plasma membrane of the marine alga Platymonas viridis

Попова, Л. Г.; Balnokin, Yu. V.

doi:10.1016/0014-5793(92)80801-m

Cited by 28 publications

(14 citation statements)

References 15 publications

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“…The existence of Na +-pumping ATPases in the plasma membrane has been postulated as one mechanism [14,25,41], On the other hand, Na +/H ÷ antiporters that could use the electrochemical H + gradient to extrude Na + from the cytosol have also been shown to be operative in the plasma membrane [ 15,27]. In this context, it might be expected that a dramatic increase in the external NaC1 concentration would lead to a concerted increase in both the H + -ATPase and the Na +/H + antiporter activities.…”

Section: Discussionmentioning

confidence: 99%

Primary structure of the plasma membrane H+-ATPase from the halotolerant alga Dunaliella bioculata

1995

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P-type ATPase-specific oligodeoxyribonucleotides were used to obtain a fragment of the H(+)-ATPase of the salt tolerant alga Dunaliella bioculata by polymerase chain reaction (PCR). This fragment served as a probe in screening a cDNA-library from this organism. The complete primary structure of the ATPase protein (DBPMA1) was deduced from sequencing a 4.7 kb cDNA clone. The protein shows highest homology to H(+)-ATPases from higher plants and fungi (43% identity, 67% similarity) but has a higher calculated molecular mass (123 kDa). The latter can be assigned mainly to an additional hydrophilic domain between transmembrane segments VI and VII and to an extended carboxyterminus. These unusual structural features of DBPMA1 are interpreted in terms of providing regulatory sites of the enzyme. Southern blot analysis suggests the presence of only a single copy of the gene in the haploid D. bioculata genome. To investigate the role of the H(+)-ATPase in the adaption of D. bioculata to different external NaCl concentrations, we employed northern blot analyses. The results indicate that the pma1 transcript level of cells growing in salinities between 0.1 and 3 M NaCl is not directly correlated with the external salt concentration.

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Section: Discussionmentioning

confidence: 99%

Primary structure of the plasma membrane H+-ATPase from the halotolerant alga Dunaliella bioculata

1995

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“…However, Na + /H + antiporters, transporting Na + out of the cytoplasm into the apoplast or the vacuole, are present in all the higher plant species investigated thus far, but conceivably expressed at higher levels both in (highly) salt tolerant monocotyledonae and dicotyledonae terrestrial plants (Benito and Rodriguez-Navarro, 2003). Na +/ H + antiport activity also occurs in plasma membranes of marine algae (Popova and Balnokin, 1992). …”

Section: Evolution Of Salt Tolerance In Terrestrial Dicotyledonae Andmentioning

confidence: 99%

Salt tolerance of halophytes, research questions reviewed in the perspective of saline agriculture

Rozema

Schat

2013

Environmental and Experimental Botany

204

131

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“…Lumen alkalization implies H + efflux out of the vesicles to the external medium. In the absence of ATP, this process reflects operation of the Na + /H + antiporter (Popova and Balnokin 1992). Addition of ATP accelerates H + efflux, thus indicating involvement of the ATPase reaction in H + translocation across the vesicle membrane.…”

Section: Resultsmentioning

confidence: 97%

The Na + -translocating ATPase in the plasma membrane of the marine microalga Tetraselmis viridis catalyzes Na + /H + exchange

Balnokin

Попова

Pagis

et al. 2004

Planta

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Our previous investigations have established that Na+ translocation across the Tetraselmis viridis plasma membrane (PM) mediated by the primary ATP-driven Na+-pump, Na+-ATPase, is accompanied by H+ counter-transport [Y.V. Balnokin et al. (1999) FEBS Lett 462:402-406]. The hypothesis that the Na+-ATPase of T. viridis operates as an Na+/H+ exchanger is tested in the present work. The study of Na+ and H+ transport in PM vesicles isolated from T. viridis demonstrated that the membrane-permeant anion NO3- caused (i) an increase in ATP-driven Na+ uptake by the vesicles, (ii) an increase in (Na(+)+ATP)-dependent vesicle lumen alkalization resulting from H+ efflux out of the vesicles and (iii) dissipation of electrical potential, deltapsi, generated across the vesicle membrane by the Na+-ATPase. The (Na(+)+ATP)-dependent lumen alkalization was not significantly affected by valinomycin, addition of which in the presence of K+ abolished deltapsi at the vesicle membrane. The fact that the Na+-ATPase-mediated alkalization of the vesicle lumen is sustained in the absence of the transmembrane deltapsi is consistent with a primary role of the Na+-ATPase in driving H+ outside the vesicles. The findings allowed us to conclude that the Na+-ATPase of T. viridis directly performs an exchange of Na+ for H+. Since the Na+-ATPase generates electric potential across the vesicle membrane, the transport stoichiometry is mNa+/nH+, where m> n.

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H⁺‐translocating ATPase and Na⁺/H⁺ antiport activities in the plasma membrane of the marine alga Platymonas viridis

Cited by 28 publications

References 15 publications

Primary structure of the plasma membrane H+-ATPase from the halotolerant alga Dunaliella bioculata

Primary structure of the plasma membrane H+-ATPase from the halotolerant alga Dunaliella bioculata

Salt tolerance of halophytes, research questions reviewed in the perspective of saline agriculture

The Na + -translocating ATPase in the plasma membrane of the marine microalga Tetraselmis viridis catalyzes Na + /H + exchange

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