Abstract
Saporin-6 is a single-chain ribosome inactivating protein (RIP) from the seeds and the leaves of Saponaria officinalis (Caryophyllaceae). Here we have identified the COOH-terminal end of mature Saporin-6 and, by cDNA sequencing, the predicted carboxyl-terminal sequence of a leaf Saporin-6 primary translation product. Our data indicate that the characterized cDNA codes for a precursor containing a 22 amino acid carboxyl-terminal extension, not present in mature Saporin-6, that shows similarity to carboxyl-terminal propeptides of vacuolar proteins, suggesting that it may be involved in protein trafficking.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Amino Acid Sequence
-
Base Sequence
-
DNA / chemistry*
-
Immunotoxins*
-
Molecular Sequence Data
-
N-Glycosyl Hydrolases*
-
Peptide Fragments / chemistry
-
Plant Proteins / chemistry
-
Plant Proteins / genetics*
-
Polymerase Chain Reaction
-
Protein Precursors / chemistry
-
Protein Precursors / genetics*
-
Ribosome Inactivating Proteins, Type 1
-
Saporins
Substances
-
Immunotoxins
-
Peptide Fragments
-
Plant Proteins
-
Protein Precursors
-
Ribosome Inactivating Proteins, Type 1
-
DNA
-
N-Glycosyl Hydrolases
-
Saporins
Associated data
-
GENBANK/D10379
-
GENBANK/D10380
-
GENBANK/D10381
-
GENBANK/D10382
-
GENBANK/D10383
-
GENBANK/D10384
-
GENBANK/S62474
-
GENBANK/S62510
-
GENBANK/X58803
-
GENBANK/X61394