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| Item Type: | Article |
|---|---|
| Title: | Molecular analysis of the interaction between cardosin A and phospholipase Dalpha |
| Creators Name: | Simoes, I., Mueller, E.C., Otto, A., Bur, D., Cheung, A.Y., Faro, C. and Pires, E. |
| Abstract: | Cardosin A is an RGD-containing aspartic proteinase from the stigmatic papillae of Cynara cardunculus L. A putative cardosin A-binding protein has previously been isolated from pollen suggesting its potential involvement in pollen-pistil interaction [Faro C, Ramalho-Santos M, Vieira M, Mendes A, Simoees I, Andrade R, Verissimo P, Lin X, Tang J & Pires E (1999) J Biol Chem 274, 28724-28729]. Here we report the identification of phospholipase Dα as a cardosin A-binding protein. The interaction was confirmed by coimmunoprecipitation studies and pull-down assays. To investigate the structural and molecular determinants involved in the interaction, pull-down assays with cardosin A and various glutathione S-transferase-fused phospholipase D{alpha} constructs were performed. Results revealed that the C2 domain of phospholipase D{alpha} contains the cardosin A-binding activity. Further assays with mutated recombinant forms of cardosin A showed that the RGD motif as well as the unprecedented KGE motif, which is structurally and charge-wise very similar to RGD, are indispensable for the interaction. Taken together our results indicate that the C2 domain of plant phospholipase Dα can act as a cardosin A-binding domain and suggest that plant C2 domains may have an additional role as RGD/KGE-recognition domains. |
| Keywords: | Aspartic Proteinases, C2 Domain, Cardosin A, Phospholipase D, RGD/KGE Sequences |
| Source: | FEBS Journal |
| ISSN: | 1742-464X |
| Publisher: | Blackwell Publishing |
| Volume: | 272 |
| Number: | 22 |
| Page Range: | 5786-5798 |
| Date: | 1 November 2005 |
| Official Publication: | https://doi.org/10.1111/j.1742-4658.2005.04967.x |
| PubMed: | View item in PubMed |
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