Characterization and Expression of Four Proline-Rich Cell Wall Protein Genes in Arabidopsis Encoding Two Distinct Subsets of Multiple Domain Proteins
Open Access
- 1 December 1999
- journal article
- Published by Oxford University Press (OUP) in Plant Physiology
- Vol. 121 (4), 1081-1091
- https://doi.org/10.1104/pp.121.4.1081
Abstract
We have characterized the molecular organization and expression of four proline-rich protein genes from Arabidopsis (AtPRPs). These genes predict two classes of cell wall proteins based on DNA sequence identity, repetitive motifs, and domain organization. AtPRP1 and AtPRP3encode proteins containing an N-terminal PRP-like domain followed by a C-terminal domain that is biased toward P, T, Y, and K.AtPRP2 and AtPRP4 represent a second, novel group of PRP genes that encode two-domain proteins containing a non-repetitive N-terminal domain followed by a PRP-like region rich in P, V, K, and C. Northern hybridization analysis indicated that AtPRP1 and AtPRP3 are exclusively expressed in roots, while transcripts encoding AtPRP2 and AtPRP4 were most abundant in aerial organs of the plant. Histochemical analyses of promoter/β-glucuronidase fusions localized AtPRP3 expression to regions of the root containing root hairs. AtPRP2 and AtPRP4expression was detected in expanding leaves, stems, flowers, and siliques. In addition, AtPRP4 expression was detected in stipules and during the early stages of lateral root formation. These studies support a model for involvement of PRPs in specifying cell-type-specific wall structures, and provide the basis for a genetic approach to dissect the function of PRPs during growth and development.Keywords
This publication has 55 references indexed in Scilit:
- Isolation of pl 4.6 extensin peroxidase from tomato cell suspension cultures and identification of Val—Tyr—Lys as putative intermolecular cross‐link siteThe Plant Journal, 1996
- Solubilization and Partial Characterization of Extensin Fragments from Cell Walls of Cotton Suspension Cultures (Evidence for a Covalent Cross-Link between Extensin and Pectin)Plant Physiology, 1995
- A new proline-rich early nodulin from Medicago truncatula is highly expressed in nodule meristematic cells.Plant Cell, 1994
- Extensin: repetitive motifs, functional sites, post‐translational codes, and phylogenyThe Plant Journal, 1994
- Comparative localization of three classes of cell wall proteinsThe Plant Journal, 1991
- Isolation and Characterization of a Proline-Rich Cell Wall Protein from Soybean SeedlingsPlant Physiology, 1990
- Characterization of two soybean repetitive proline-rich proteins and a cognate cDNA from germinated axes.Plant Cell, 1989
- Developmentally regulated expression of soybean proline-rich cell wall protein genes.Plant Cell, 1989
- A copia-like transposable element family in Arabidopsis thalianaNature, 1988
- A simple method for displaying the hydropathic character of a proteinJournal of Molecular Biology, 1982