C-terminal deletion analysis of plant plasma membrane H(+)-ATPase: yeast as a model system for solute transport across the plant plasma membrane.

Regenberg, Birgitte; Villalba, José M.; Lanfermeijer, Frank C.; Palmgren, Michael G.

doi:10.1105/tpc.7.10.1655

Cited by 82 publications

(81 citation statements)

References 40 publications

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“…Similar results have been obtained with the AHA2 ATPase of Arabidopsis thaliana [44,50]. Since the complete + and truncated plant H -ATPases are expressed at similar levels in yeast ( [50]; J.R. Perez-Castifieira, unpublished results), an explanation for this behaviour might + be that complete plant H -ATPases are not fully functional unless properly activated [50,56]. Although the mechanisms of activation have not been clarified, it is + plausible that plant H -ATPases never get fully activated in the yeast heterologous system and therefore, only by deletion of the inhibitory domain can the plant enzymes be functional in yeast.…”

Section: Discussionsupporting

confidence: 72%

“…The complete BHA1 gene is not functional but a truncated version lacking the autoinhibitory domain at the carboxyl terminus can support yeast growth. Similar results have been obtained with the AHA2 ATPase of Arabidopsis thaliana [44,50]. Since the complete + and truncated plant H -ATPases are expressed at similar levels in yeast ( [50]; J.R. Perez-Castifieira, unpublished results), an explanation for this behaviour might + be that complete plant H -ATPases are not fully functional unless properly activated [50,56].…”

Section: Discussionsupporting

confidence: 65%

“…As the plant enzyme could not experience proper regulation in yeast cells, we have expressed both the completed BHA1 H+-ATPase and a truncated version lacking the last 98 amino acids and therefore the autoinhibitory domain [50,56]. As indicated in Fig.…”

Section: Bha1 Encodes a Functional And Regulated Proton Pumpmentioning

confidence: 99%

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Localization of plasma membrane H+-ATPase in nodules of Phaseolus vulgaris L.

et al. 1996

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Legume nodules have specialized transport functions for the exchange of carbon and nitrogen compounds between bacteroids and root cells. Plasma membrane-type (vanadate-sensitive) H+-ATPase energizes secondary active transporters in plant cells and it could drive exchanges across peribacteroidal and plasmatic membranes. A nodule cDNA corresponding to a major isoform of Phaseolus vulgaris H+-ATPase (designated BHA1) has been cloned. BHA1 is a functional proton pump because after removal of its inhibitory domain and can complement a yeast mutant unable to synthesize a H+-ATPase. BHA1 is not nodule-specific, since it is also expressed in roots of uninfected plants. It belongs to the subfamily of plasma membrane H+-ATPases defined by the Arabidopsis AHA1, AHA2 and AHA3 genes and the tobacco PMA4 and corn MHA2 genes. In situ hybridization in nodule sections indicates high expression of BHA1 limited to uninfected cells. These results were confirmed by immunocytochemistry. The relatively low expression of plasma membrane-type H+-ATPase in Rhizobium-infected cells put a note of caution on the origin of the vanadate-sensitive ATPase described in preparations of peribacteroidal membranes. Also, our results indicate that active transport in symbiotic nodules is most intense at the plasma membrane of uninfected cells and support a specialized role of uninfected tissue for nitrogen transport.

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Section: Discussionsupporting

confidence: 72%

Section: Discussionsupporting

confidence: 65%

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Localization of plasma membrane H+-ATPase in nodules of Phaseolus vulgaris L.

et al. 1996

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“…Olsson et al (1995) suggested that the C-terminal autoinhibitory domain of the PM H + -ATPase might have multiple regulatory sites. Regenberg et al (1995) examined this possibility by a C-terminal deletion analysis of the PM H + -ATPase of Arabidopsis AHA2 carried out in a yeast expression system. The removal of the final 38 C-terminal amino acid residues produced only a decrease in the K m for ATP; an increase in the V max was brought about when an additional 12 residues were removed from the C-terminus.…”

Section: Photosynthesis-dependent Acceleration Of the Activity Of Thementioning

confidence: 99%

Photosynthetic control of the plasma membrane H + -ATPase in Vallisneria leaves. I. Regulation of activity during light-induced membrane hyperpolarization

Harada

Okazaki

Takagi

2002

Planta

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In mesophyll cells of the aquatic angiosperm Vallisneria gigantea Graebner, red, blue, or blue plus far-red light induced a typical membrane hyperpolarization, whereas far-red light alone had little effect. Both N,N'-dicyclohexylcarbodiimide, a potent inhibitor of H+-ATPase, and carbonylcyanide m-chlorophenylhydrazone, an uncoupler, produced a considerable membrane depolarization in the dark-adapted cells and a complete suppression of the light-induced hyperpolarization. Although 3-(3',4'-dichlorophenyl)-1,1-dimethylurea (DCMU), an inhibitor of photosynthetic electron transport, did not affect the membrane potential in darkness, it completely inhibited the light-induced membrane hyperpolarization. In vivo illumination of the leaves with red light caused a substantial decrease in the Km for ATP, not only of the vanadate-sensitive ATP-hydrolyzing activity in leaf homogenate, but also of the ATP-dependent H+-transporting activity in plasma membrane (PM) vesicles isolated from the leaves by aqueous polymer two-phase partitioning methods. The effects of red light were negated by the presence of DCMU during illumination. In vivo illumination with far-red light had no effect on the Km for ATP of H+-transporting activity. These results strongly suggest that an electrogenic component in the membrane potential of the mesophyll cell is generated by the PM H+-ATPase, and that photosynthesis-dependent modulation of the enzymatic activity of the PM H+-ATPase is involved in the light-induced membrane hyperpolarization.

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“…The PM H + -ATPase is predicted to be a transmembrane protein of approximately 100 kDa, the amino and carboxyl termini of which are on the cytoplasmic side of the PM (Michelet and Boutry 1995). The carboxyl-terminal (C-terminal) region of the PM H + -ATPase contains an autoinhibitory domain of about 50 amino acids (Regenberg et al 1995). When the C-terminal autoinhibitory domain was removed by proteolysis in vitro, both a decrease in the K m for ATP and an increase in the V max of the PM H + -ATPase activity were observed (Palmgren et al 1990(Palmgren et al , 1991.…”

Section: Introductionmentioning

confidence: 99%

Photosynthetic control of the plasma membrane H + -ATPase in Vallisneria leaves. II. Presence of putative isogenes and a protein equipped with a C-terminal autoinhibitory domain

Harada

Fukuhara

Takagi

2002

Planta

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In vitro treatment with trypsin of plasma membrane (PM) vesicles isolated from the leaves of Vallisneria gigantea Graebner, an aquatic monocot, produced a marked decrease in the Km for ATP and an increase in the Vmax of H+-transporting activity. Concomitantly, the removal of 8 kDa of the C-terminal domain from the 94-kDa PM H+-ATPase was confirmed by immunoblotting using different kinds of polyclonal antibody. Three partial clones of putative PM H+-ATPase genes (Vga1, 2, and 3) were isolated from leaves by reverse transcription polymerase chain reaction. Northern blotting analysis revealed that the expression level of Vga3 was high and that of the other two genes was much lower. The H+-transporting activity of PM vesicles was substantially suppressed in the presence of inorganic phosphate (Pi), which has been supposed to be a noncompetitive inhibitor of the PM H+-ATPase, coincident with an increase in the Km for ATP and a decrease in the Vmax. After treatment of the isolated PM vesicles with trypsin, the inhibitory effect of Pi was no longer evident. This result indicates that Pi inhibited the activity through the C-terminal autoinhibitory domain of the PM H+-ATPase. Furthermore, Pi increased the Km for ATP of the H+-transporting activity in the PM vesicles isolated from both dark-adapted and red-light-irradiated leaves. The results suggest that regulation of the Km for ATP through the operation of photosynthesis is independent of regulation through the cytoplasmic level of Pi.

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C-terminal deletion analysis of plant plasma membrane H(+)-ATPase: yeast as a model system for solute transport across the plant plasma membrane.

Cited by 82 publications

References 40 publications

Localization of plasma membrane H+-ATPase in nodules of Phaseolus vulgaris L.

Localization of plasma membrane H+-ATPase in nodules of Phaseolus vulgaris L.

Photosynthetic control of the plasma membrane H + -ATPase in Vallisneria leaves. I. Regulation of activity during light-induced membrane hyperpolarization

Photosynthetic control of the plasma membrane H + -ATPase in Vallisneria leaves. II. Presence of putative isogenes and a protein equipped with a C-terminal autoinhibitory domain

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