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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
A New Member of Plant CS-lyases
A CYSTINE LYASE FROM ARABIDOPSIS THALIANA*
Patrik R.
Jones ,
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.
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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Copyright © 2003 by the American Society for Biochemistry and Molecular Biology.
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