1988
DOI: 10.1007/bf00425691
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Analysis of the expression of extensin and p33-related cell wall proteins in carrot and soybean

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Cited by 62 publications
(52 citation statements)
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“…Another valuable component of the defense response to pathogens appears to be the degradation of preexisting mRNAs whose products may interfere with the protective mechanisms against the pathogen. The reinforcement of the cell wall after infection or wounding involves the increased transcription of hydroxyproline-rich glycoprotein and proline-rich protein genes (Lawton and Lamb, 1987;Tierney et al, 1988). The encoded proteins are rich in tyrosine and are capable of insolubilization in the wall, presumably by isodityrosine cross-links.…”
Section: Discussionmentioning
confidence: 99%
See 1 more Smart Citation
“…Another valuable component of the defense response to pathogens appears to be the degradation of preexisting mRNAs whose products may interfere with the protective mechanisms against the pathogen. The reinforcement of the cell wall after infection or wounding involves the increased transcription of hydroxyproline-rich glycoprotein and proline-rich protein genes (Lawton and Lamb, 1987;Tierney et al, 1988). The encoded proteins are rich in tyrosine and are capable of insolubilization in the wall, presumably by isodityrosine cross-links.…”
Section: Discussionmentioning
confidence: 99%
“…We have hypothesized that the synthesis of the PvPRPI protein is reduced during the defense response because of its low potential for wall strengthening by isodityrosine cross-linking (Sheng et al, 1991). In contrast, mRNAs encoding specific praline-rich proteins and hydroxyproline-rich glycoproteins with greater cross-linking potentials accumulate during the defense response (Lawton and Lamb, 1987;Tierney et al, 1988). The importance of cell wall structural protein regulation in plant defense is supported by recent work showing that elicitortreated soybean cells undergo a very rapid oxidative crosslinking of cell wall proteins (Bradley et al, 1992).…”
Section: Introductionmentioning
confidence: 99%
“…Finally, the diagnostic Ser-Hyp 4 peptide (Smith et al, 1986) enabled identification of the first extensin (Chen and Varner, 1985) and PRP cDNAs (Hong et al, 1987;Tierney et al, 1988;Datta et al, 1989) as bona fide proteins with the hallmark of other structural proteins, most notably collagen, which is also Hyp rich and the major structural fibrillar protein of animals. Collagen polypeptides occur in an extended poly-Pro-II lefthanded helical conformation, which was also con-firmed in carrot extensin by further circular dichroism spectra (van Holst and Varner, 1984), with evidence for the role of carbohydrate in maintaining the backbone conformation (Stafstrom and Staehelin, 1986).…”
Section: The Extensin Superfamily Over 5 Decadesmentioning
confidence: 99%
“…Since the discovery of cell wall protein in 1960 (Dougall and Shimbayashi, 1960;Lamport and Northcote, 1960b), the hydroxy-Pro-rich glycoprotein field, referred to generically as HRGPs, has blossomed from having only one family member (extensin; Lamport, 1963), to three (extensin, arabinogalactan protein [AGP; Yariv et al, 1962;Aspinall et al, 1969;Fincher et al, 1974], and solanaceous lectins [Allen and Neuberger, 1973]), then four (Pro-rich proteins, [PRPs; Chen and Varner, 1985;Hong et al, 1987;AveryhartFullard et al, 1988;Tierney et al, 1988;Wilson et al, 1994]) and more. We now realize that this (super)family represents a continuum of peptide periodicity and glycosylation (Kieliszewski and Lamport, 1994); perusal of the Arabidopsis genome suggests that conserved features of HRGPs, in particular their arabinosyl-O-Hyp and arabinogalactosyl-O-Hyp glycomodules, are widespread in secreted proteins ranging from phytocyanins and systemins to fasciclins and glycerophosphodiesterases (Pearce et al, 1991;Borner et al, 2002;Johnson et al, 2003;Kieliszewski et al, 2010;Showalter et al, 2010).…”
mentioning
confidence: 99%
“…Pro-rich proteins (PRPs) represent one of five families of structural cell wall proteins that have been identified in higher plants (for review, see Carpita and Gibeaut, 1993;Showalter, 1993;Cassab, 1998). PRPs were first identified as proteins that accumulate in the cell wall in response to physical damage (Chen and Varner, 1985;Tierney et al, 1988) and have subsequently been shown to be temporally regulated during plant development. PRP gene expression is associated with early stages of legume root nodule formation (Franssen et al, 1987;van de Wiel et al, 1990;Wilson et al, 1994), soybean seedling, leaf, stem, and seed coat development (Hong et al, 1989;Kleis-San Francisco and Tierney, 1990;Lindstrom and Vodkin, 1991;Ye et al, 1991), bean seedling growth (Sheng et al, 1991), and with early stages of tomato fruit development (Santino et al, 1997).…”
mentioning
confidence: 99%