PMID- 12482758
OWN - NLM
STAT- MEDLINE
DCOM- 20030422
LR  - 20210206
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 278
IP  - 8
DP  - 2003 Feb 21
TI  - Identification of a novel protein with guanylyl cyclase activity in Arabidopsis 
      thaliana.
PG  - 6490-4
AB  - 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 
      Mg(2+)-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.
FAU - Ludidi, Ndiko
AU  - Ludidi N
AD  - University of the Western Cape, Department of Biotechnology, Bellville, Private 
      Bag X17, 7535, South Africa.
FAU - Gehring, Chris
AU  - Gehring C
LA  - eng
PT  - Journal Article
DEP - 20021212
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - EC 4.6.1.2 (Guanylate Cyclase)
RN  - H2D2X058MU (Cyclic GMP)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Arabidopsis/*enzymology/genetics
MH  - Cyclic GMP/*metabolism
MH  - Genome, Plant
MH  - Guanylate Cyclase/chemistry/genetics/*metabolism
MH  - Humans
MH  - Molecular Sequence Data
MH  - Sequence Alignment
MH  - Sequence Homology, Amino Acid
EDAT- 2002/12/17 04:00
MHDA- 2003/04/23 05:00
CRDT- 2002/12/17 04:00
PHST- 2002/12/17 04:00 [pubmed]
PHST- 2003/04/23 05:00 [medline]
PHST- 2002/12/17 04:00 [entrez]
AID - S0021-9258(20)86648-4 [pii]
AID - 10.1074/jbc.M210983200 [doi]
PST - ppublish
SO  - J Biol Chem. 2003 Feb 21;278(8):6490-4. doi: 10.1074/jbc.M210983200. Epub 2002 
      Dec 12.