Autor: |
Luigia Pazzagli, Barbara Pantera, Lara Carresi, Camilla Zoppi, Thelma Pertinhez, Alberto Spisni, Stefania Tegli, Aniello Scala, Gianni Cappugi |
Zdroj: |
Cell Biochemistry & Biophysics; Mar2006, Vol. 44 Issue 3, p512-521, 10p |
Abstrakt: |
The ascomycete Ceratocystis fimbriata, the causal agent of "canker stain disease," secretes a protein of 12.4 kDa that elicits phytoalexin synthesis and plant cell death. This protein, named cerato-platanin (CP), is also locatedin the cell walls of ascospores, hyphae, and conidia; it contains four cysteines (S-S bridged) and is moderately hydrophobic. The cp gene consists of a single exon and has 42 bp codifying for a signal peptide of 14 residues.The recombinant protein was obtained by cloning the cp gene of the mature protein in Escherichia coli (BL21), and a refolding step was needed to achieve the native active form. In the European Molecular Biology data bank, CPis reported as the first member of the CP family; this is the first example of an set of secreted fungal proteins whose primary structure is very similar. Nonetheless, the data also revealed some structural and functional featuresthat make CP similar to proteins of the hydrophobin family. [ABSTRACT FROM AUTHOR] |
Databáze: |
Complementary Index |
Externí odkaz: |
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