Molecular cloning and characterization of cDNA encoding cardosin B, an aspartic proteinase accumulating extracellularly in the transmitting tissue of Cynara cardunculus L.

• Type: Article in International Scientific Journal
• Date: 2001

Authors

Vieira, M (Author) Other; Pissarra, J (Author) FCUP; Verissimo, P (Author) Other; Castanheira, P (Author) Other; Costa, Y (Author) Other; Pires, E (Author) Other; Faro, C (Author) Other

Journal

Title: Plant Molecular Biology

Vol. 45

Pages: 529-539

ISSN: 0167-4412

Publisher: Springer Nature

Indexing

ISI Web of Knowledge - 45 Citations

Scopus - 46 Citations

Scientific classification

FOS: Natural sciences > Biological sciences

Other information

Authenticus ID: P-000-WAX

DOI: 10.1023/a:1010675015318

Abstract (EN): Cardosins A and B are related aspartic proteinases from the pistils of Cynara cardunculus L., whose milk-clotting activity has been exploited for the manufacture of cheese. Here we report the cloning of cardosin B cDNA and its organ, tissue and cytological localization. The cDNA-derived amino acid sequence has 73% similarity with that of cardosin A and displays several distinguishing features. Cardosin B mRNA was detected in young inflorescences but not in pistils of fully opened inflorescences, indicating that its expression is developmentally regulated. The proteinase, however, accumulates in the pistil until the later stages of floral development. Immunocytochemistry with a monospecific antibody localized cardosin B to the cell wall and extracellular matrix of the floral transmitting tissue. The location of cardosin B in the pistil is therefore clearly different from that of cardosin A, which was found at protein storage vacuoles of the stigmatic papillae and has been suggested to be involved in RGD-mediated proteolytic mechanisms. In view of these results the possible functions of cardosin B in the transmitting tissue are discussed.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 11