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A Saporin-6 cDNA containing a precursor sequence coding for a carboxyl-terminal extension
L Benatti1, G Nitti, M Solinas
1Department of Biotechnology, San Raffaele Research Institute, Milano, Italy.
FEBS Letters
|October 21, 1991
Summary
Researchers identified the COOH-terminal end of Saporin-6, a ribosome inactivating protein (RIP). A precursor form contains a carboxyl-terminal extension, potentially involved in protein trafficking within the plant cell.
Area of Science:
- Biochemistry
- Molecular Biology
- Plant Science
Background:
- Saporin-6 is a single-chain ribosome inactivating protein (RIP) found in Saponaria officinalis.
- Ribosome inactivating proteins can inhibit protein synthesis by depurinating ribosomal RNA.
Purpose of the Study:
- To identify the COOH-terminal end of mature Saporin-6.
- To determine the carboxyl-terminal sequence of the leaf Saporin-6 primary translation product.
- To investigate potential protein trafficking mechanisms for Saporin-6.
Main Methods:
- cDNA sequencing
- Analysis of protein sequences
- Comparison with known protein motifs
Main Results:
- The COOH-terminal end of mature Saporin-6 was identified.
- cDNA sequencing revealed a precursor form of leaf Saporin-6.
- This precursor contains a 22 amino acid carboxyl-terminal extension not found in the mature protein.
Conclusions:
- The carboxyl-terminal extension shares similarity with vacuolar protein propeptides.
- This suggests a role for the extension in mediating protein trafficking of Saporin-6.
- Further research is needed to elucidate the precise function of this extension in Saponaria officinalis.