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Vol. 273, Issue 2, 689-692, January 9, 1998

COMMUNICATION
Characterization of a cDNA Encoding the Thylakoidal Processing Peptidase from Arabidopsis thaliana
IMPLICATIONS FOR THE ORIGIN AND CATALYTIC MECHANISM OF THE ENZYME

Balbir K. Chaal, Ruth M. Mould^§, Adrian C. Barbrook, John C. Gray^§, and Christopher J. Howe

From the Cambridge Center for Molecular Recognition,  Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 1QW, United Kingdom and the ^§ Department of Plant Sciences, University of Cambridge, Downing Street, Cambridge CB2 3EA, United Kingdom

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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Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.

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