Abstract
We have isolated and sequenced partial cDNA clones that encode SO-6, a ribosome-inactivating protein from Saponaria officinalis. A cDNA library was constructed from the leaves of this plant and screened with synthetic oligonucleotide probes representing various portions of the protein. The deduced amino acid sequence shows the signal peptide and a coding region virtually accounting for the entire amino acid sequence of SO-6. The sequence reveals regions of similarity to other ribosome-inactivating proteins, especially in a region of the molecule where critical amino acid residues might participate in the active site.
MeSH terms
-
Amino Acid Sequence
-
Base Sequence
-
Cloning, Molecular
-
Cysteine Endopeptidases
-
DNA / genetics*
-
DNA / isolation & purification
-
DNA Restriction Enzymes
-
Immunotoxins*
-
Molecular Sequence Data
-
N-Glycosyl Hydrolases*
-
Nucleic Acid Hybridization
-
Oligonucleotide Probes
-
Peptide Fragments
-
Plant Proteins / genetics*
-
Plant Proteins / pharmacology
-
Ribosome Inactivating Proteins, Type 1
-
Ribosomes / drug effects*
-
Saporins
Substances
-
Immunotoxins
-
Oligonucleotide Probes
-
Peptide Fragments
-
Plant Proteins
-
Ribosome Inactivating Proteins, Type 1
-
DNA
-
DNA Restriction Enzymes
-
N-Glycosyl Hydrolases
-
Saporins
-
Cysteine Endopeptidases
-
clostripain