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J Biol Chem, Vol. 273, Issue 49, 32739-32745, December 4, 1998
From the Faculty of Pharmaceutical Sciences, Laboratory of
Molecular Biology and Biotechnology in Research Center of Medicinal
Resources, Chiba University, Yayoi-cho 1-33, Inage-ku, Chiba
263-8522, Japan
Serine acetyltransferase (SATase; EC 2.3.1.30),
which catalyzes the formation of
O-acetyl-L-serine (OAS) from acetyl-CoA and
L-serine, plays a regulatory role in the biosynthesis of
cysteine by its property of feedback inhibition by cysteine in bacteria and certain plants. Three cDNA clones encoding SATase isoforms (SAT-c, SAT-p, and SAT-m) have been isolated from Arabidopsis thaliana. However, the significance of the feedback regulation has not yet been clear in these different isoforms of SATase from A. thaliana. We constructed the overexpression vectors for
cDNAs encoding three SATase isoforms of A. thaliana and
analyzed the inhibition of SATase activity by cysteine using the
recombinant SATase proteins. In the case of SAT-c, the activity was
feedback-inhibited by a low concentration of cysteine (the
concentration that inhibits 50% activity; IC50 = 1.8 µM). By contrast, SAT-p and SAT-m were feedback
inhibition-insensitive isozymes. We also determined the subcellular
localization of three SATase isozymes by the transient expression of
fusion proteins of each SATase N-terminal region with jellyfish green
fluorescent protein (GFP) in 4-week-old Arabidopsis leaves. The
SAT-c-GFP fusion protein was stayed in cytosol, whereas SAT-p-GFP and
SAT-m-GFP fusion proteins were localized in chloroplasts and in
mitochondria, respectively. These results suggest that these three
SATase isoforms, which are localized in the different organelles, are
subjected to different feedback regulation, presumably so as to play
the particular roles for the production of OAS and cysteine in
Arabidopsis cells. Regulatory circuit of cysteine biosynthesis in the
plant cells is discussed.
Isoform-dependent Differences in Feedback Regulation
and Subcellular Localization of Serine Acetyltransferase Involved
in Cysteine Biosynthesis from Arabidopsis thaliana
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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