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

• Tipo: Artigo em Revista Científica Internacional
• Data: 2001

Autores

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

Revista

Título: Plant Molecular Biology

Vol. 45

Páginas: 529-539

ISSN: 0167-4412

Editora: Springer Nature

Indexação

ISI Web of Knowledge - 45 Citações

Scopus - 46 Citações

Classificação Científica

FOS: Ciências exactas e naturais > Ciências biológicas

Outras Informações

ID Authenticus: 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.

Idioma: Inglês

Tipo (Avaliação Docente): Científica

Nº de páginas: 11