| Autor: |
Chaal, B K, Mould, R M, Barbrook, A C, Gray, J C, Howe, C J |
| Zdroj: |
Journal of Biological Chemistry; January 1998, Vol. 273 Issue: 2 p689-92, 4p |
| Abstrakt: |
We have identified and sequenced a cDNA containing a complete open reading frame for a putative 340-amino acid precursor of the thylakoidal processing peptidase from Arabidopsis thaliana. The predicted amino acid sequence of the protein includes regions highly conserved among Type I leader peptidases and indicates that the enzyme uses a serine-lysine catalytic dyad mechanism. Phylogenetic analysis indicated a common ancestry of the enzyme with those from oxygenic photosynthetic prokaryotes, suggesting that the cDNA encoded the chloroplast enzyme. The catalytic domain was overexpressed in Escherichia coli, generating a product capable of cleaving the thylakoid-transfer domain from a chloroplast protein. Antibodies to the overexpressed polypeptide cross-reacted with a 30-kDa thylakoid membrane protein. |
| Databáze: |
Supplemental Index |
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