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Volume 35 Issue 10
Oct.  2008
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Isolation and characterization of two genes encoding polygalacturonase-inhibiting protein from Populus deltoides

doi: 10.1016/S1673-8527(08)60084-3
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  • Corresponding author: E-mail address: mrhuang@njfu.edu.cn (Minren Huang)
  • Received Date: 2008-02-23
  • Accepted Date: 2008-07-18
  • Rev Recd Date: 2008-07-14
  • Available Online: 2008-10-18
  • Publish Date: 2008-10-20
  • Polygalacturonase-inhibiting proteins (PGIPs) are extracellular proteins that belong to the leucine-rich repeat (LRR) protein superfamily. PGIPs inhibit fungal polygalacturonases (PGs) and promote accumulation of oligogalacturonides, which activate plant defense responses. PGIPs play important roles in resistance to infection of pathogens. In this study, reverse transcriptase-polymerase chain reaction (RT-PCR) and RNA ligase-mediated rapid amplification of cDNA ends (RLM-RACE) were used to isolate the full-length PGIP cDNA from Populus deltoides (GenBank accession no. of PdPGIP2 and PdPGIP4: EF684913 and EF684912). Domain analysis revealed that the deduced amino acid sequences of PdPGIP2 and PdPGIP4 had a typical PGIP topology. Phylogenetic analysis of known PGIPs indicated that the two PdPGIPs were clustered to the defense-related PGIP clade. Using real-time RT-PCR, the expression patterns of the two PdPGIPs following treatment with a fungal pathogen and defense-related signaling molecules were studied. The expression levels ofPdPGIP2 and PdPGIP4 were both up-regulated when inoculated with the phytopathogenic fungus Marssonina brunnea. Therefore, it was proposed that the two PGIPs might be involved in the resistance to Marssonina brunnea in P. deltoides.
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  • [1]
    Baumberger, N., Doesseger, B., Guyot, R. et al. Plant Physiol., 131 (2003),pp. 1313-1326
    [2]
    D'Ovidio, R., Raiola, A., Capodicasa, C. et al. Characterization of the complex locus of bean encoding polygalacturonase-inhibiting proteins reveals subfunctionalization for defense against fungi and insects Plant Physiol., 135 (2004),pp. 2424-2435
    [3]
    de Lorenzo, G., D'Ovidio, R., Cervone, F. The role of polygalacturonase-inhibiting proteins (PGIPs) in defense against pathogenic fungi Annu. Rev. Phytopathol., 39 (2001),pp. 313-335
    [4]
    di Matteo, A., Bonivento, D., Tsernoglou, D. et al. Polygalacturonase-inhibiting protein (PGIP) in plant defence: A structural view Phytochemistry, 67 (2006),pp. 528-533
    [5]
    di Matteo, A., Federici, L., Mattei, B. et al. The crystal structure of polygalacturonase-inhibiting protein (PGIP), a leucine-rich repeat protein involved in plant defense Proc. Natl. Acad. Sci. USA, 100 (2003),pp. 10124-10128
    [6]
    Federici, L., di Matteo, A., Fernandez-Recio, J. et al. Polygalacturonase inhibiting proteins: Players in plant innate immunity? Trends Plant Sci., 11 (2006),pp. 65-70
    [7]
    Ferrari, S., Vairo, D., Ausubel, F.M. et al. Plant Cell, 15 (2003),pp. 93-106
    [8]
    Ferrari, S., Galletti, R., Vairo, D. et al. Mol. Plant Microbe Interact., 19 (2006),pp. 931-936
    [9]
    Gamboa, A., Paez-Valencia, J., Acevedo, G.F. et al. Biochem. Biophys. Res. Commun., 288 (2001),pp. 1018-1026
    [10]
    Guyon, V., Tang, W.H., Monti, M.M. et al. Antisense phenotypes reveal a role for SHY, a pollen-specific leucine-rich repeat protein, in pollen tube growth Plant J., 39 (2004),pp. 643-654
    [11]
    Isshiki, A., Akimitsu, K., Yamamoto, M. et al. Mol. Plant Microbe Interact., 14 (2001),pp. 749-757
    [12]
    Jang, S., Lee, B., Kim, C. et al. Plant Mol. Biol., 53 (2003),pp. 357-369
    [13]
    Joubert, D.A., Slaughter, A.R., Kemp, G. et al. Transgenic Res., 15 (2006),pp. 687-702
    [14]
    Leckie, F., Mattei, B., Capodicasa, C. et al. The specificity of polygalacturonase-inhibiting protein (PGIP): A single amino acid substitution in the solvent-exposed beta-strand/beta-turn region of the leucine-rich repeats (LRRs) confers a new recognition capability EMBO J., 18 (1999),pp. 2352-2363
    [15]
    Manfredini, C., Sicilia, F., Ferrari, S. et al. Physiol. Mol. Plant Pathol., 67 (2005),pp. 108-115
    [16]
    Oeser, B., Heidrich, P.M., Muller, U. et al. Fungal Genet. Biol., 36 (2002),pp. 176-186
    [17]
    Page, R.D. TreeView: An application to display phylogenetic trees on personal computers Comput. Appl. Biosci., 12 (1996),pp. 357-358
    [18]
    Powell, A.L., van Kan, J., ten Have, A. et al. Transgenic expression of pear PGIP in tomato limits fungal colonization Mol. Plant Microbe Interact., 13 (2000),pp. 942-950
    [19]
    ten Have, A., Mulder, W., Visser, J. et al. Mol. Plant Microbe Interact., 11 (1998),pp. 1009-1016
    [20]
    Thompson, J.D., Gibson, T.J., Plewniak, F. et al. The CLUSTAL_X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools Nucleic Acids Res., 25 (1997),pp. 4876-4882
    [21]
    Tuskan, G.A., Difazio, S., Jansson, S. et al. Science, 313 (2006),pp. 1596-1604
    [22]
    Vandesompele, J., de Preter, K., Pattyn, F. et al. Accurate normalization of real-time quantitative RT-PCR data by geometric averaging of multiple internal control genes Genome Biol., 3 (2002)
    [23]
    Vorwerk, S., Somerville, S., Somerville, C. The role of plant cell wall polysaccharide composition in disease resistance Trends Plant Sci., 9 (2004),pp. 203-209
    [24]
    Worrall, D., Elias, L., Ashford, D. et al. A carrot leucine-rich-repeat protein that inhibits ice recrystallization Science, 282 (1998),pp. 115-117
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