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J. Biol. Chem., Vol. 278, Issue 8, 6490-6494, February 21, 2003
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From the University of the Western Cape, Department of
Biotechnology, Bellville, Private Bag X17, 7535, South Africa
Guanylyl cyclases (GCs) catalyze the
formation of the second messenger guanosine 3',5'-cyclic monophosphate
(cGMP) from guanosine 5'-triphosphate (GTP). While many cGMP-mediated
processes in plants have been reported, no plant molecule with GC
activity has been identified. When the Arabidopsis thaliana
genome is queried with GC sequences from cyanobacteria, lower and
higher eukaryotes no unassigned proteins with significant similarity
are found. However, a motif search of the A. thaliana
genome based on conserved and functionally assigned amino acids in the
catalytic center of annotated GCs returns one candidate that also
contains the adjacent glycine-rich domain typical for GCs. In this
molecule, termed AtGC1, the catalytic domain is in the N-terminal part.
AtGC1 contains the arginine or lysine that participates in hydrogen
bonding with guanine and the cysteine that confers substrate
specificity for GTP. When AtGC1 is expressed in Escherichia
coli, cell extracts yield >2.5 times more cGMP than control
extracts and this increase is not nitric oxide dependent. Furthermore,
purified recombinant AtGC1 has Mg2+-dependent
GC activity in vitro and >3 times less adenylyl cyclase activity when assayed with ATP as substrate in the absence of GTP.
Catalytic activity in vitro proves that AtGC1 can function either as a monomer or homo-oligomer. AtGC1 is thus not only the first
functional plant GC but also, due to its unusual domain organization, a
member of a new class of GCs.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EBI Data Bank with accession number(s) AAM51559.
Identification of a Novel Protein with Guanylyl Cyclase Activity
in Arabidopsis thaliana*
*
This work was supported by the National Research Foundation
of South Africa.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.
To whom correspondence should be addressed: University of the
Western Cape, Dept. of Biotechnology, Bellville, Private Bag X17, 7535, South Africa. Tel.: 27-21-959-2199; Fax: 27-21-959-1349; E-mail:
cgehring@uwc.ac.za.
Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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