The developmental expression of the asparagus intracellular PR protein (AoPR1) gene correlates with sites of phenylpropanoid biosynthesis

The RNA Hydrolysis and the Cytokinin Binding Activities of PR-10 Proteins Are Differently Performed by Two Isoforms of the Pru p 1 Peach Major Allergen and Are Possibly Functionally Related

“…It is noteworthy that also the expression of aoPR1, encoding a PR-10 protein from asparagus (Asparagus officinalis), was shown to temporally and spatially correlate with the expression of genes coding for enzymes of the phenylpropanoid pathway. Moreover, the promoter of aoPR1 gene contains sequence motifs similar to those found in the phenylpropanoid genes (Warner et al, 1994). These data suggest that PR-10 proteins act in concert with the phenylpropanoid pathway, which is known to be involved in several plant defense responses (Dixon et al, 2002) or that phenylpropanoid intermediates regulate PR-10 gene expression (Warner et al, 1994).…”

“…Moreover, the promoter of aoPR1 gene contains sequence motifs similar to those found in the phenylpropanoid genes (Warner et al, 1994). These data suggest that PR-10 proteins act in concert with the phenylpropanoid pathway, which is known to be involved in several plant defense responses (Dixon et al, 2002) or that phenylpropanoid intermediates regulate PR-10 gene expression (Warner et al, 1994). PR-10 proteins have been considered a multifunctional protein family, encompassing different functional subfamilies that share homology in tertiary structure in spite of low sequence similarity.…”

“…They were first identified in parsley (Petroselinum crispum; Somssich et al, 1988) and later isolated from several plant species and tissues (Matton and Brisson, 1989;Crowell et al, 1992;Warner et al, 1994;Breda et al, 1996;Midoh and Iwata, 1996;Huang et al, 1997;Lo et al, 1999;Yu et al, 2000;Wu et al, 2003). PR-10 proteins are typically small (from 155-163 residues) cytoplasmic proteins with acidic pI (Liu and Ekramoddoullah, 2006).…”

Lupinus albus L. Pathogenesis-Related Proteins That Show Similarity to PR-10 Proteins

“…In tobacco plants, it was found that during the systemic response to tobacco mosaic virus infection, the distribution of PR-1 proteins in the noninoculated leaves was limited to the extracellular spaces surrounding vascular bundles as well as in vacuoles of crystal idioblasts (Dixon et al, 1991). More recently, studies of developmental expression of the A. officinalis AoPRl gene in transgenic tobacco plants have shown that the strongest expression was in the expanding secondary xylem of the stems as they became lignified (Warner et al, 1994 To our knowledge, no ultrastructural studies on the localization of PR-10 proteins have been made so far, b u t it has been proposed that these proteins act intracellularly, since n o signal sequences typical of extracellular proteins are encoded by the genes (Somssich et al, 1988). However, the lupin proteins seem to be accumulated in the cell wall, as are the tobacco PR-1 proteins.…”

The Potential ofBetv1Homologues, a Nuclear Multigene Family, as Phylogenetic Markers in Flowering Plants

“…A role was suggested for these proteins as enzymes of the core phenylpropanoid pathway that are involved in the synthesis of cell-wall structural molecules, pigments, UV-light protectants, chemical attractants, and antimicrobial phytoalexins (Warner et al, 1994). Along the same lines, it was proposed by Yazaki et al (1995) that the LEDI-1 protein from Lithospermum erythrorhizon might play a significant role in the induction of secondary metabolism, such as shikonin production.…”