Negative and positive regulation of a novel proline-rich protein mRNA by fungal elicitor and wounding.

The structure and expression of a cDNA clone (PvPRP1) isolated from a cDNA library prepared from bean (Phaseolus vulgaris) cells treated with fungal elicitor have been characterized. Sequence analysis of the 1.1 kb insert revealed a complete open reading frame which encodes a 32 kDa protein. The protein resembles other proline-rich proteins in plants but possesses several unique features: (i) the N-terminal half of the protein is proline rich and contains three identical repeats of Pro-Val-His-Pro-Pro-Val-Lys-Pro-Pro-Val and six related repeats; (ii) the proline-rich region contains two tracts of six histidine residues; and (iii) the C-terminal half is low in proline and lacks repeats. Genomic blotting experiments suggest the presence of a single PvPRP1 gene as well as more distantly related genes within the bean genome. A dramatic decrease in PvPRP1 mRNA levels occurs within 2 h of elicitor treatment of cell cultures. The PvPRP1 mRNA is present at a moderate level in hypocotyls. Upon wounding, the mRNA level initially decreases over 5 h and then accumulates over 25 h to levels which are higher than the basal level in unwounded hypocotyls. Based on the similarity to other proline-rich proteins with repeated motifs, including the presence of a putative signal peptide, it is likely that the PvPRP1 protein is targetted to the cell wall. The expression of the PvPRP1 gene appears to be integrated with the remodeling of the plant cell wall during the defense response.