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Gene Review

VGDH2  -  Probable pectinesterase/pectinesterase...

Arabidopsis thaliana

Synonyms: VANGUARD 1 homolog 2
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Disease relevance of VGDH2

  • Annotation predicts that QRT1 encodes a pectin methylesterase (PME), and enzymatic assays of QRT1 expressed in Escherichia coli indicate that QRT1 has PME activity [1].

High impact information on VGDH2

  • Functional interruption of VGD1 reduced PME activity in the pollen to 82% of the wild type and greatly retarded the growth of the pollen tube in the style and transmitting tract, resulting in a significant reduction of male fertility [2].
  • Pectin methylesterase (PME) and invertase are key enzymes in plant carbohydrate metabolism [3].
  • Application of an exogenous PME induces thickening of the apical cell wall and inhibits pollen tube growth [4].
  • Screening a Nicotiana tabacum pollen cDNA library yielded a pollen-specific PME, NtPPME1, containing a pre-region and a pro-region [4].
  • Functional classification of the expressed genes reveals that those involved in cellular biogenesis such as polygalacturonase, pectate lyase, and pectin methylesterase make up more than 40% of the total transcripts [5].

Biological context of VGDH2

  • Our results, in combination with several known expressed sequences tags (ESTs), indicate that the Arabidopsis genome contains at least 12 PME-related genes [6].
  • These results showed that B. cinerea possessed more than one PME-encoding gene and that BCPME1 is an important determinant of B. cinerea virulence [7].
  • In this paper, we report the characterization of AtPME3, a new PME-related gene of 4kb in length that we have mapped on Chromosome III [6].
  • In order to better define the biological role of these isoenzymes in plant cell growth and differentiation, we undertook molecular studies on the PME-encoding genes in Arabidopsis thaliana [6].
  • PME action produces pectin with different structural and functional properties, having an important role in plant physiology [8].

Anatomical context of VGDH2

  • In addition to providing experimental data that help resolve the significance and function of the pro-region, our results give insight into the mechanism by which PME and its pro-region regulate the cell wall dynamics of growing pollen tubes [4].

Associations of VGDH2 with chemical compounds


Analytical, diagnostic and therapeutic context of VGDH2

  • Affinity chromatography on resin-bound PMEI can also be used to concentrate and detect residual PME activity in fruit and vegetable products [8].


  1. Separation of Arabidopsis Pollen Tetrads Is Regulated by QUARTET1, a Pectin Methylesterase Gene. Francis, K.E., Lam, S.Y., Copenhaver, G.P. Plant Physiol. (2006) [Pubmed]
  2. VANGUARD1 encodes a pectin methylesterase that enhances pollen tube growth in the Arabidopsis style and transmitting tract. Jiang, L., Yang, S.L., Xie, L.F., Puah, C.S., Zhang, X.Q., Yang, W.C., Sundaresan, V., Ye, D. Plant Cell (2005) [Pubmed]
  3. Structural insights into the target specificity of plant invertase and pectin methylesterase inhibitory proteins. Hothorn, M., Wolf, S., Aloy, P., Greiner, S., Scheffzek, K. Plant Cell (2004) [Pubmed]
  4. Pectin methylesterase, a regulator of pollen tube growth. Bosch, M., Cheung, A.Y., Hepler, P.K. Plant Physiol. (2005) [Pubmed]
  5. Use of serial analysis of gene expression technology to reveal changes in gene expression in Arabidopsis pollen undergoing cold stress. Lee, J.Y., Lee, D.H. Plant Physiol. (2003) [Pubmed]
  6. Characterization of the pectin methylesterase-like gene AtPME3: a new member of a gene family comprising at least 12 genes in Arabidopsis thaliana. Micheli, F., Holliger, C., Goldberg, R., Richard, L. Gene (1998) [Pubmed]
  7. Disruption of Botrytis cinerea pectin methylesterase gene Bcpme1 reduces virulence on several host plants. Valette-Collet, O., Cimerman, A., Reignault, P., Levis, C., Boccara, M. Mol. Plant Microbe Interact. (2003) [Pubmed]
  8. Pectin methylesterase inhibitor. Giovane, A., Servillo, L., Balestrieri, C., Raiola, A., D'Avino, R., Tamburrini, M., Ciardiello, M.A., Camardella, L. Biochim. Biophys. Acta (2004) [Pubmed]
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