PMID- 17520012
OWN - NLM
STAT- MEDLINE
DCOM- 20100429
LR  - 20240326
IS  - 1932-6203 (Electronic)
IS  - 1932-6203 (Linking)
VI  - 2
IP  - 5
DP  - 2007 May 23
TI  - The Arabidopsis thaliana brassinosteroid receptor (AtBRI1) contains a domain that 
      functions as a guanylyl cyclase in vitro.
PG  - e449
LID - e449
AB  - BACKGROUND: Guanylyl cyclases (GCs) catalyze the formation of the second 
      messenger guanosine 3',5'-cyclic monophosphate (cGMP) from guanosine 
      5'-triphosphate (GTP). Cyclic GMP has been implicated in an increasing number of 
      plant processes, including responses to abiotic stresses such as dehydration and 
      salt, as well as hormones. PRINCIPLE FINDINGS: Here we used a rational search 
      strategy based on conserved and functionally assigned residues in the catalytic 
      centre of annotated GCs to identify candidate GCs in Arabidopsis thaliana and 
      show that one of the candidates is the brassinosteroid receptor AtBR1, a leucine 
      rich repeat receptor like kinase. We have cloned and expressed a 114 amino acid 
      recombinant protein (AtBR1-GC) that harbours the putative catalytic domain, and 
      demonstrate that this molecule can convert GTP to cGMP in vitro. CONCLUSIONS: Our 
      results suggest that AtBR1 may belong to a novel class of GCs that contains both 
      a cytosolic kinase and GC domain, and thus have a domain organisation that is not 
      dissimilar to that of atrial natriuretic peptide receptors, NPR1 and NPR2. The 
      findings also suggest that cGMP may have a role as a second messenger in 
      brassinosteroid signalling. In addition, it is conceivable that other proteins 
      containing the extended GC search motif may also have catalytic activity, thus 
      implying that a significant number of GCs, both in plants and animals, remain to 
      be discovered, and this is in keeping with the fact that the single cellular 
      green alga Chlamydomonas reinhardtii contains over 90 annotated putative CGs.
FAU - Kwezi, Lusisizwe
AU  - Kwezi L
AD  - Department of Biotechnology, University of the Western Cape, Bellville, South 
      Africa.
FAU - Meier, Stuart
AU  - Meier S
FAU - Mungur, Lyndon
AU  - Mungur L
FAU - Ruzvidzo, Oziniel
AU  - Ruzvidzo O
FAU - Irving, Helen
AU  - Irving H
FAU - Gehring, Chris
AU  - Gehring C
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20070523
PL  - United States
TA  - PLoS One
JT  - PloS one
JID - 101285081
RN  - 0 (DNA Primers)
RN  - 0 (Receptors, Steroid)
RN  - EC 4.6.1.2 (Guanylate Cyclase)
RN  - H2D2X058MU (Cyclic GMP)
SB  - IM
MH  - Amino Acid Sequence
MH  - Arabidopsis/*metabolism
MH  - Base Sequence
MH  - Catalytic Domain
MH  - Cyclic GMP/metabolism
MH  - DNA Primers
MH  - Guanylate Cyclase/chemistry/*metabolism
MH  - Molecular Sequence Data
MH  - Mutagenesis, Site-Directed
MH  - Receptors, Steroid/chemistry/genetics/*metabolism
MH  - Sequence Homology, Amino Acid
MH  - Signal Transduction
PMC - PMC1867859
COIS- Competing Interests: The authors have declared that no competing interests exist.
EDAT- 2007/05/24 09:00
MHDA- 2007/05/24 09:01
PMCR- 2007/05/23
CRDT- 2007/05/24 09:00
PHST- 2007/02/26 00:00 [received]
PHST- 2007/04/19 00:00 [accepted]
PHST- 2007/05/24 09:00 [pubmed]
PHST- 2007/05/24 09:01 [medline]
PHST- 2007/05/24 09:00 [entrez]
PHST- 2007/05/23 00:00 [pmc-release]
AID - 07-PONE-RA-00833R1 [pii]
AID - 10.1371/journal.pone.0000449 [doi]
PST - epublish
SO  - PLoS One. 2007 May 23;2(5):e449. doi: 10.1371/journal.pone.0000449.