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Gene Review

AVP1  -  Pyrophosphate-energized vacuolar membrane...

Arabidopsis thaliana

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Disease relevance of AVP1

  • AVP1 overexpression results in increased cell division at the onset of organ formation, hyperplasia, and increased auxin transport [1].
  • This result supports the hypothesis that overexpression of H(+)-PPase causes the accumulation of Na(+) in vacuoles instead of in the cytoplasm and avoids the toxicity of excessive Na(+) in plant cells [2].
  • The heterologous expression of TsVP in the yeast mutant ena1 suppressed Na(+) hypersensitivity and demonstrated the function of TsVP as an H(+)-PPase [2].

Psychiatry related information on AVP1

  • Transgenic Arabidopsis plants overexpressing the wheat vacuolar Na(+)/H(+) antiporter TNHX1 and H(+)-PPase TVP1 are much more resistant to high concentrations of NaCl and to water deprivation than the wild-type strains [3].

High impact information on AVP1

  • Recent work demonstrates that AVP1 plays an important role in root development through the facilitation of auxin fluxes [4].
  • The phenotypes of the AVP1 transgenic plants suggest that increasing the vacuolar proton gradient results in increased solute accumulation and water retention [5].
  • Since the heterologously expressed pump is indistinguishable from the native plant enzyme with respect to PPi hydrolysis, H+ translocation, activation by potassium, and selective inhibition by calcium and 1,1-diphosphonates, it is concluded that all of the known catalytic functions of the enzyme map to the one subunit encoded by AVP [6].
  • Since the tonoplast H(+)-PPase appears to be constituted of one polypeptide species and genomic Southern analyses indicate that the gene encoding the Mr 80,800 polypeptide is present in only a single copy in the genome of Arabidopsis, it is suggested that the H(+)-PPase has been cloned in its entirety [7].
  • The H(+)-PPase, like the V-type H(+)-ATPase, is abundant and ubiquitous in the vacuolar membranes of plant cells, and both enzymes make a substantial contribution to the transtonoplast H(+)-electrochemical potential difference [7].

Biological context of AVP1


Anatomical context of AVP1

  • These findings suggest that this novel type H(+)-PPase resides on the Golgi apparatus rather than the vacuolar membrane [10].
  • Purification of the electron-dense vacuoles using iodixanol density gradients indicated a preferential localization of the H(+)-PPase and the V-H(+)-ATPase activities in addition to high concentrations of PP(i) and short and long chain polyphosphate, but lack of markers for mitochondria and chloroplasts [11].
  • The labeling pattern of the vacuolar proton-pyrophosphatase, considered as a marker for the organelle, changed accompanying the structural changes of the acidocalcisomes, and the enzyme showed an apparently lower proton-transporting activity when measured in digitonin-permeabilized promastigotes [12].

Associations of AVP1 with chemical compounds


Other interactions of AVP1

  • The differences between AVP2 and AVP1 provide the first indication that plant V-PPases from the same organism fall into two distinct categories [14].

Analytical, diagnostic and therapeutic context of AVP1


  1. Arabidopsis H+-PPase AVP1 regulates auxin-mediated organ development. Li, J., Yang, H., Peer, W.A., Richter, G., Blakeslee, J., Bandyopadhyay, A., Titapiwantakun, B., Undurraga, S., Khodakovskaya, M., Richards, E.L., Krizek, B., Murphy, A.S., Gilroy, S., Gaxiola, R. Science (2005) [Pubmed]
  2. Cloning of an H+-PPase gene from Thellungiella halophila and its heterologous expression to improve tobacco salt tolerance. Gao, F., Gao, Q., Duan, X., Yue, G., Yang, A., Zhang, J. J. Exp. Bot. (2006) [Pubmed]
  3. Overexpression of wheat Na+/H+ antiporter TNHX1 and H+-pyrophosphatase TVP1 improve salt- and drought-stress tolerance in Arabidopsis thaliana plants. Brini, F., Hanin, M., Mezghani, I., Berkowitz, G.A., Masmoudi, K. J. Exp. Bot. (2007) [Pubmed]
  4. Up-regulation of a H+-pyrophosphatase (H+-PPase) as a strategy to engineer drought-resistant crop plants. Park, S., Li, J., Pittman, J.K., Berkowitz, G.A., Yang, H., Undurraga, S., Morris, J., Hirschi, K.D., Gaxiola, R.A. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  5. Drought- and salt-tolerant plants result from overexpression of the AVP1 H+-pump. Gaxiola, R.A., Li, J., Undurraga, S., Dang, L.M., Allen, G.J., Alper, S.L., Fink, G.R. Proc. Natl. Acad. Sci. U.S.A. (2001) [Pubmed]
  6. Heterologous expression of plant vacuolar pyrophosphatase in yeast demonstrates sufficiency of the substrate-binding subunit for proton transport. Kim, E.J., Zhen, R.G., Rea, P.A. Proc. Natl. Acad. Sci. U.S.A. (1994) [Pubmed]
  7. Molecular cloning and sequence of cDNA encoding the pyrophosphate-energized vacuolar membrane proton pump of Arabidopsis thaliana. Sarafian, V., Kim, Y., Poole, R.J., Rea, P.A. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
  8. Pollen-specific regulation of vacuolar H+-PPase expression by multiple cis-acting elements. Mitsuda, N., Takeyasu, K., Sato, M.H. Plant Mol. Biol. (2001) [Pubmed]
  9. Cloning and characterization of a wheat vacuolar cation/proton antiporter and pyrophosphatase proton pump. Brini, F., Gaxiola, R.A., Berkowitz, G.A., Masmoudi, K. Plant Physiol. Biochem. (2005) [Pubmed]
  10. Novel type Arabidopsis thaliana H(+)-PPase is localized to the Golgi apparatus. Mitsuda, N., Enami, K., Nakata, M., Takeyasu, K., Sato, M.H. FEBS Lett. (2001) [Pubmed]
  11. The polyphosphate bodies of Chlamydomonas reinhardtii possess a proton-pumping pyrophosphatase and are similar to acidocalcisomes. Ruiz, F.A., Marchesini, N., Seufferheld, M., Govindjee, n.u.l.l., Docampo, R. J. Biol. Chem. (2001) [Pubmed]
  12. Dynamics of polymorphism of acidocalcisomes in Leishmania parasites. Miranda, K., Docampo, R., Grillo, O., Franzen, A., Attias, M., Vercesi, A., Plattner, H., Hentschel, J., de Souza, W. Histochem. Cell Biol. (2004) [Pubmed]
  13. Roles of basic residues and salt-bridge interaction in a vacuolar H(+)-pumping pyrophosphatase (AVP1) from Arabidopsis thaliana. Zancani, M., Skiera, L.A., Sanders, D. Biochim. Biophys. Acta (2007) [Pubmed]
  14. AVP2, a sequence-divergent, K(+)-insensitive H(+)-translocating inorganic pyrophosphatase from Arabidopsis. Drozdowicz, Y.M., Kissinger, J.C., Rea, P.A. Plant Physiol. (2000) [Pubmed]
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