Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
9604383 | Journal of Biotechnology | 2005 | 4 Pages |
Abstract
In the present communication, we report on the expression and characterisation in Escherichia coli of mutant derivatives of saporin, a type 1 ribosome-inactivating protein from Saponaria officinalis L. The effects of substitution of Glu 176 with Lys and those of deletion of 19 amino acids at the C-terminal were evaluated both in vivo, testing the influence of expressed proteins on bacterial growth and in vitro measuring their N-glycosidase and supercoiled DNA relaxation activities. Results indicate that both modifications of the wild-type protein abolish its toxicity to bacterial cells and impair its enzymatic activity on polynucleotide substrates, either RNA or DNA.
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Authors
Eugenia Pittaluga, Anna Poma, Adele Tucci, Laura Spanò,