Studies on the Higher Plant Calmodulin-Stimulated ATPase

Evans, David; Askerlund, Per; Boyce, Joy M.; Briars, Sally-Anne.; Coates, David; Coates, J. B.; Cooke, David T.; Theodoulou, F. L.

doi:10.1007/978-1-4615-3442-6_4

Cited by 10 publications

(10 citation statements)

References 40 publications

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“…In particular, the presence of CaM in purified PM fractions has been documented in a few instances (Collinge and Trewavas, 1989;Evans et al, 1992). The results reported in this paper show that the PM isolated from radish seedlings contains substantial amounts of tightly bound CaM that can be at least partially removed by drastic treatment with the calcium chelator EDTA.…”

Section: Dlscusslonsupporting

confidence: 56%

“…The relatively low and quite variable stimulation of the plant PM Ca2+ pump by exogenous CaM might depend on the presence of CaM in the PM preparations. In fact, the presence of tightly bound CaM in PM preparations from plants is documented (Collinge and Trewavas, 1989;Evans et al, 1992); moreover, the activation of the PM Caz+ pump by exogenous CaM could be increased by treatments of the PM fraction with the Ca2+ chelating agent EGTA (Williams et al, 1990).…”

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confidence: 99%

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Controlled Proteolysis Activates the Plasma Membrane Ca2+ Pump of Higher Plants (A Comparison with the Effect of Calmodulin in Plasma Membrane from Radish Seedlings)

Rasi‐Caldogno¹,

Carnelli²,

Michelis³

1993

Plant Physiol.

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The effects of calmodulin and of controlled trypsin treatments on the activity of the Caz+ pump were investigated in plasma membrane purified from radish (Raphanus sativus 1.) seedlings. Treatment of the plasma membrane with ethylenediaminetetraacetate (EDTA), which removed about two-thirds of the plasma membrane-associated calmodulin, markedly increased the stimulation of the Caz+ pump by calmodulin. In EDTA-treated plasma membrane, stimulation by calmodulin of the Caz+ pump activity was maximal at low free Caz+ (2-5 p~) and decreased with the increase of free CaZ+ concentration. l h e CaZ+ pump activity was stimulated also by a controlled treatment of the plasma membrane with trypsin: the effect of trypsin treatment depended on the concentration of both trypsin and plasma membrane proteins and on the duration of incubation. Stimulation of the CaZ+ pump activity by trypsin treatment of the plasma membrane was similar to that induced by calmodulin both in extent and in dependence on the free CaZ+ concentration in the assay medium. Moreover, the Caz+ pump of trypsin-treated plasma membrane was insensitive to further stimulation by calmodulin, suggesting that limited proteolysis preferentially cleaves a regulatory domain of the enzyme that is involved in its activation by calmodulin.In plant cells, the extrusion of Ca2+ from the cytoplasm to the apoplast is catalyzed by a Mg-ATP-dependent Ca2+ pump. During the last few years, the transport and hydrolytic activities of the plant PM Ca2+ pump have been characterized in some detail both in native PM vesicles and in proteoliposomes reconstituted with the solubilized and partially purified enzyme (reviewed in Briskin, 1990; Evans et al., 1991;De Michelis et al., 1992a). The most striking characteristics of the plant PM Ca2+ pump are its ability to use ITP or GTP besides ATP as a substrate (Williams et al., 1990; Camelli et al., 1992) and its high sensitivity to inhibition by fluorescein derivatives such as erythrosin B (Rasi-Caldogno et al., 1987, This work was supported by a grant of the Italian Ministry for University and Scientific and Technologic Research (40% quote) and by the Italian Ministry of Agriculture in the framework of the project 'Resistenze genetiche delle piante agrarie agli stress biotici ed abiotici."

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Section: Dlscusslonsupporting

confidence: 56%

mentioning

confidence: 99%

Controlled Proteolysis Activates the Plasma Membrane Ca2+ Pump of Higher Plants (A Comparison with the Effect of Calmodulin in Plasma Membrane from Radish Seedlings)

Rasi‐Caldogno¹,

Carnelli²,

Michelis³

1993

Plant Physiol.

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“…Since it has been shown that the PM Ca 2+ -ATPase retains CaM associated with it during PM isolation (Robinson et al, 1988;Williams et al, 1990;Evans et al, 1992;Rasi-Caldogno et al, 1993;Olbe and Sommarin, 1998), these data indicate that the amount of CaM associated with the PM Ca 2+ -ATPase is increased by OG treatment. To test this hypothesis, we took advantage of our previous finding that the Ca 2+ -ATPase is the major CaM binding protein in the PM (Rasi-Caldogno et al, 1995;Bonza et al, 1998).…”

Section: Effects Of Og On the Activity Of The Pm Ca 2+ -Atpasementioning

confidence: 83%

Involvement of the Plasma Membrane Ca²⁺‐ATPase in the Short‐Term Response of Arabidopsis thaliana Cultured Cells to Oligogalacturonides

et al. 2004

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Treatment of Arabidopsis thaliana cells with oligogalacturonides (OG) initiates a transient production of reactive oxygen species (ROS), the concentration of which in the medium peaks after about 20 min of treatment. The analysis of OG effects on Ca (2+) fluxes shows that OG influence both Ca (2+) influx and Ca (2+) efflux (measured as (45)Ca (2+) fluxes) in a complex way. During the first 10 - 15 min, OG stimulate Ca (2+) influx and decrease its efflux, while at successive times of treatment, OG cause an increase of Ca (2+) efflux and a slight decrease of its influx. Treatment with sub- micro M concentrations of eosin yellow (EY), which selectively inhibits the Ca (2+)-ATPase of plasma membrane (PM), completely prevents the OG-induced increase in Ca (2+) efflux. EY also suppresses the transient feature of OG-induced ROS accumulation, keeping the level of ROS in the medium high. The biochemical analysis of PM purified from OG-treated cells indicates that treatment with OG for 15 to 45 min induces a significant decrease in Ca (2+)-ATPase activation by exogenous calmodulin (CaM), and markedly increases the amount of CaM associated with the PM. During the same time span, OG do not influence the expression of At-ACA8, the main isoform of PM Ca (2+)-ATPase in suspension-cultured A. thaliana cells, and of CaM genes. Overall, the reported results demonstrate that the PM Ca (2+)-ATPase is involved in the response of plant cells to OG and is essential in regulation of the oxidative burst.

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“…These values fall within the range of those reported for different isoforms of PMCA (Caride et al 1999) and set At-ACA8 in the group of slow-response, high-affinity type IIB Ca 2þ -ATPases. The slow rate of CaM release may give account of the high level of CaM-Ca 2þ -ATPase commonly found in isolated PM (Dainese et al 1997, Evans et al 1992, Kurosaki and Kaburaki 1994, Olbe et al 1997, Robinson et al 1988, Romani et al 2004, Williams et al 1990). In fact, the thermal and mechanical stress to which plant materials are exposed immediately before membrane isolation would rise cytosolic free Ca 2þ concentration (Sanders et al 2002) promoting formation of the CaM-Ca 2þ -ATPase complex, the dissociation of which would occur only very slowly during the following steps performed on ice.…”

Section: Kinetics Of Interaction Between Pm Ca 2+ -Atpase and Cammentioning

confidence: 99%

“…Stimulation of Ca 2þ -ATPase activity by exogenous CaM in isolated PM vesicles is low or even undetectable unless endogenous CaM is removed by extensive washing with strong Ca 2þ chelators (Dainese et al 1997, Evans et al 1992, Kurosaki and Kaburaki 1994, Olbe et al 1997, Robinson et al 1988, Romani et al 2004, Williams et al 1990). Moreover, the PM Ca 2þ -ATPase efficiently binds CaM in overlay experiments (Askerlund 1997, Bonza et al 1998, Dainese et al 1997, Olbe and Sommarin 1998, Rasi-Caldogno et al 1995 and tightly binds to CaM-agarose (Bonza et al 1998).…”

Section: Introductionmentioning

confidence: 99%

Calmodulin/Ca²⁺‐ATPase interaction at the Arabidopsis thaliana plasma membrane is dependent on calmodulin isoform showing isoform‐specific Ca²⁺ dependencies

Luoni

Bonza

Michelis

2006

Physiologia Plantarum

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Arabidopsis thaliana plasma membrane (PM) Ca2+‐ATPase is a type IIB P‐type ATPase, which binds calmodulin (CaM) to an autoinhibitory N‐terminal domain. Here, we took advantage of the fact that PM isolated from cultured cells mainly contains At‐ACA8, the first cloned A. thaliana PM Ca2+‐ATPase, to analyse its interaction with CaM in detail. Analysis of the ability of different peptides designed from At‐ACA8 N‐terminus to compete with the native protein for binding of bovine brain CaM (bbCaM) showed that peptide 41I‐T63 had the same affinity of the native protein [apparent dissociation constant (KD) at 10 µM free Ca2+ about 25 nM], thus localizing At‐ACA8 CaM‐binding site within this sequence. The interaction of At‐ACA8 N‐terminus with bbCaM, as determined by surface plasmon resonance, was rapid, and slowly but was fully reversible. Analysis of Ca2+‐ATPase activation as a function of the concentration of different isoforms of A. thaliana CaM showed that Ca2+‐ATPase is activated to similar extent by bbCaM and by different isoforms of homologous CaM. However, the affinity for the divergent A. thaliana isoform CaM8 was lower than that for canonical CaM isoforms such as A. thaliana CaM2, CaM4 and CaM6 or bbCaM. The apparent KD for CaM isoforms of the native enzyme increased with the decrease of free Ca2+ concentration, suggesting that enzyme conformation is affected by Ca2+. Binding of CaM isoforms to At‐ACA8 N‐terminus was affected differently by free Ca2+ concentration, suggesting that plant CaMs may have different affinities for Ca2+.

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Studies on the Higher Plant Calmodulin-Stimulated ATPase

Cited by 10 publications

References 40 publications

Controlled Proteolysis Activates the Plasma Membrane Ca2+ Pump of Higher Plants (A Comparison with the Effect of Calmodulin in Plasma Membrane from Radish Seedlings)

Controlled Proteolysis Activates the Plasma Membrane Ca2+ Pump of Higher Plants (A Comparison with the Effect of Calmodulin in Plasma Membrane from Radish Seedlings)

Involvement of the Plasma Membrane Ca²⁺‐ATPase in the Short‐Term Response of Arabidopsis thaliana Cultured Cells to Oligogalacturonides

Calmodulin/Ca²⁺‐ATPase interaction at the Arabidopsis thaliana plasma membrane is dependent on calmodulin isoform showing isoform‐specific Ca²⁺ dependencies

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Studies on the Higher Plant Calmodulin-Stimulated ATPase

Cited by 10 publications

References 40 publications

Controlled Proteolysis Activates the Plasma Membrane Ca2+ Pump of Higher Plants (A Comparison with the Effect of Calmodulin in Plasma Membrane from Radish Seedlings)

Controlled Proteolysis Activates the Plasma Membrane Ca2+ Pump of Higher Plants (A Comparison with the Effect of Calmodulin in Plasma Membrane from Radish Seedlings)

Involvement of the Plasma Membrane Ca2+‐ATPase in the Short‐Term Response of Arabidopsis thaliana Cultured Cells to Oligogalacturonides

Calmodulin/Ca2+‐ATPase interaction at the Arabidopsis thaliana plasma membrane is dependent on calmodulin isoform showing isoform‐specific Ca2+ dependencies

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Product

Resources

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Involvement of the Plasma Membrane Ca²⁺‐ATPase in the Short‐Term Response of Arabidopsis thaliana Cultured Cells to Oligogalacturonides

Calmodulin/Ca²⁺‐ATPase interaction at the Arabidopsis thaliana plasma membrane is dependent on calmodulin isoform showing isoform‐specific Ca²⁺ dependencies