PMID- 23835195
OWN - NLM
STAT- MEDLINE
DCOM- 20140221
LR  - 20211021
IS  - 1478-811X (Electronic)
IS  - 1478-811X (Linking)
VI  - 11
DP  - 2013 Jul 8
TI  - The Arabidopsis thaliana proteome harbors undiscovered multi-domain molecules 
      with functional guanylyl cyclase catalytic centers.
PG  - 48
LID - 10.1186/1478-811X-11-48 [doi]
AB  - BACKGROUND: Second messengers link external cues to complex physiological 
      responses. One such messenger, 3',5'-cyclic guanosine monophosphate (cGMP), has 
      been shown to play a key role in many physiological responses in plants. However, 
      in higher plants, guanylyl cyclases (GCs), enzymes that generate cGMP from 
      guanosine-5'-triphosphate (GTP) have remained elusive until recently. GC search 
      motifs constructed from the alignment of known GCs catalytic centers form 
      vertebrates and lower eukaryotes have led to the identification of a number of 
      plant GCs that have been characterized in vitro and in vivo.Presentation of the 
      hypothesis. Recently characterized GCs in Arabidopsis thaliana contributed to the 
      development of search parameters that can identify novel candidate GCs in plants. 
      We hypothesize that there are still a substantial number (> 40) of multi-domain 
      molecules with potentially functional GC catalytic centers in plants that remain 
      to be discovered and characterized. TESTING THE HYPOTHESIS: The hypothesis can be 
      tested, firstly, by computational methods constructing 3D models of selected GC 
      candidates using available crystal structures as templates. Homology modeling 
      must include substrate docking that can provide support for the structural 
      feasibility of the GC catalytic centers in those candidates. Secondly, 
      recombinant peptides containing the GC domain need to be tested in in vitro GC 
      assays such as the enzyme-linked immune-sorbent assay (ELISA) and/or in mass 
      spectrometry based cGMP assays. In addition, quantification of in vivo cGMP 
      transients with fluorescent cGMP-reporter assays in wild-type or selected mutants 
      will help to elucidate the biological role of novel GCs. Implications of the 
      hypothesis. If it turns out that plants do harbor a large number of functional GC 
      domains as part of multi-domain enzymes, then major new insights will be gained 
      into the complex signal transduction pathways that link cGMP to fundamental 
      processes such as ion transport and homeostasis, biotic and abiotic stress 
      responses as well as cGMP-dependent responses to hormones.
FAU - Wong, Aloysius
AU  - Wong A
AD  - Division of Biological and Environmental Science and Engineering, 4700 King 
      Abdullah University of Science and Technology, Thuwal 23955-6900, Kingdom of 
      Saudi Arabia.
FAU - Gehring, Chris
AU  - Gehring C
LA  - eng
PT  - Journal Article
DEP - 20130708
PL  - England
TA  - Cell Commun Signal
JT  - Cell communication and signaling : CCS
JID - 101170464
RN  - 0 (Arabidopsis Proteins)
RN  - 0 (Proteome)
RN  - 86-01-1 (Guanosine Triphosphate)
RN  - EC 4.6.1.2 (Guanylate Cyclase)
RN  - H2D2X058MU (Cyclic GMP)
SB  - IM
MH  - Arabidopsis/*enzymology
MH  - Arabidopsis Proteins/chemistry/*metabolism
MH  - Catalytic Domain
MH  - Cyclic GMP/metabolism
MH  - Guanosine Triphosphate/metabolism
MH  - Guanylate Cyclase/chemistry/*metabolism
MH  - Molecular Docking Simulation
MH  - Proteome
PMC - PMC3726316
EDAT- 2013/07/10 06:00
MHDA- 2014/02/22 06:00
PMCR- 2013/07/08
CRDT- 2013/07/10 06:00
PHST- 2013/05/04 00:00 [received]
PHST- 2013/07/05 00:00 [accepted]
PHST- 2013/07/10 06:00 [entrez]
PHST- 2013/07/10 06:00 [pubmed]
PHST- 2014/02/22 06:00 [medline]
PHST- 2013/07/08 00:00 [pmc-release]
AID - 1478-811X-11-48 [pii]
AID - 10.1186/1478-811X-11-48 [doi]
PST - epublish
SO  - Cell Commun Signal. 2013 Jul 8;11:48. doi: 10.1186/1478-811X-11-48.