Please use this identifier to cite or link to this item: https://hdl.handle.net/10316/8121
Title: Molecular analysis of the interaction between cardosin A and phospholipase Dα
Authors: Simões, Isaura 
Mueller, Eva-Christina 
Otto, Albrecht 
Bur, Daniel 
Cheung, Alice Y. 
Faro, Carlos 
Pires, Euclides 
Issue Date: 2005
Citation: FEBS Journal. 272:22 (2005) 5786-5798
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 pollen2013pistil interaction [Faro C, Ramalho-Santos M, Vieira M, Mendes A, Simões I, Andrade R, Verissimo P, Lin X, Tang J & Pires E (1999) J Biol Chem274, 28724201328729]. Here we report the identification of phospholipase D03B1 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 D03B1 constructs were performed. Results revealed that the C2 domain of phospholipase D03B1 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 D03B1 can act as a cardosin A-binding domain and suggest that plant C2 domains may have an additional role as RGD/KGE-recognition domains.
URI: https://hdl.handle.net/10316/8121
DOI: 10.1111/j.1742-4658.2005.04967.x
Rights: openAccess
Appears in Collections:FCTUC Ciências da Vida - Artigos em Revistas Internacionais

Files in This Item:
File Description SizeFormat
obra.pdf627.2 kBAdobe PDFView/Open
Show full item record

SCOPUSTM   
Citations

34
checked on Nov 11, 2022

WEB OF SCIENCETM
Citations 5

33
checked on May 2, 2023

Page view(s) 20

641
checked on Apr 9, 2024

Download(s) 5

3,985
checked on Apr 9, 2024

Google ScholarTM

Check

Altmetric

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.