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Originally published In Press as doi:10.1074/jbc.M212207200 on January 13, 2003

J. Biol. Chem., Vol. 278, Issue 12, 10291-10296, March 21, 2003
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A New Member of Plant CS-lyases
A CYSTINE LYASE FROM ARABIDOPSIS THALIANA*

Patrik R. JonesDagger , Tomofumi Manabe, Motoko Awazuhara, and Kazuki Saito§

From the Department of Molecular Biology and Biotechnology, Graduate school of Pharmaceutical Sciences, Chiba University, CREST of Japan Science and Technology Corporation, Yayoi-cho 1-33, Inage-ku, Chiba 263-8522, Japan

Cystine lyases catalyze the breakdown of L-cystine to thiocysteine, pyruvate, and ammonia. Until now there are no reports of the identification of a plant cystine lyase at a molecular level, and it is not clear what biological role this class of enzymes have in plants. A cystine lyase was isolated from Brassica oleracea (L.), and partial amino acid sequencing allowed the corresponding full-length cDNA (BOCL3) to be cloned. The deduced amino acid sequence of BOCL3 showed highest homology to the deduced amino acid sequences of several Arabidopsis thaliana genes annotated as tyrosine aminotransferase-like, including a coronatine, jasmonic acid, and salt stress-inducible gene, CORI3 (78.8% identity), and the unidentified rooty/superroot1 gene (44.8% identity). A full-length expressed sequence tag clone of CORI3 was obtained and recombinant CORI3 was synthesized in Escherichia coli. Isolated recombinant CORI3 catalyzed a cystine lyase reaction, but no aminotransferase reactions. The present study identifies, for the first time, a cystine lyase from plants at a molecular level and redefines the functional assignment of the only functionally identified member of a group of A. thaliana genes annotated as tyrosine aminotransferase-like.


* This work was supported in part by grants-in-aid for Scientific Research from the Ministry of Education, Science, Sports and Culture, Japan and by CREST of Japan Science and Technology.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EBI Data Bank with accession number(s) AY187682.

Dagger Recipient of a postdoctoral fellowship from the Japan Society for the Promotion of Science.

§ To whom correspondence should be addressed. Tel.: 81-43-290-2904; Fax: 81-43-290-2905; E-mail: ksaito@p.chiba-u.ac.jp.


Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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