Characterization of a cDNA encoding the thylakoidal processing peptidase from Arabidopsis thaliana -: Implications for the origin and catalytic mechanism of the enzyme
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作者:
Chaal, BK
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机构:Univ Cambridge, Dept Biochem, Cambridge CB2 1QW, England
Chaal, BK
Mould, RM
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机构:Univ Cambridge, Dept Biochem, Cambridge CB2 1QW, England
Mould, RM
Barbrook, AC
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机构:Univ Cambridge, Dept Biochem, Cambridge CB2 1QW, England
Barbrook, AC
Gray, JC
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机构:Univ Cambridge, Dept Biochem, Cambridge CB2 1QW, England
Gray, JC
Howe, CJ
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机构:Univ Cambridge, Dept Biochem, Cambridge CB2 1QW, England
Howe, CJ
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[1] Univ Cambridge, Dept Biochem, Cambridge CB2 1QW, England
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.