Characterization of a cDNA encoding the thylakoidal processing peptidase from Arabidopsis thaliana -: Implications for the origin and catalytic mechanism of the enzyme

被引:41
作者
Chaal, BK
Mould, RM
Barbrook, AC
Gray, JC
Howe, CJ
机构
[1] Univ Cambridge, Dept Biochem, Cambridge CB2 1QW, England
[2] Univ Cambridge, Cambridge Ctr Mol Recognit, Cambridge CB2 1QW, England
[3] Univ Cambridge, Dept Plant Sci, Cambridge CB2 3EA, England
关键词
D O I
10.1074/jbc.273.2.689
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
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页码:689 / 692
页数:4
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