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Article Addendum

Plant Nucleotide Cyclases: An Increasingly Complex and Growing Family

Stuart Meier, Cathal Seoighe, Lusisizwe Kwezi, Helen Irving and Chris Gehring

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Second messengers have a key role in linking environmental stimuli to physiological responses. One such messenger, cGMP, has long been known to be critical to many different processes in higher plants while guanylyl cyclases (GCs), enzymes that catalyse the formation of cGMP from GTP have largely remained elusive. This is somewhat surprising considering that the unicellular green alga Chlamydomonas reinhardtii contains > 90 annotated GCs. We have recently shown (PLoS ONE 2(5): e449) that a recombinant cytoplasmic domain of the Arabidopsis brassinosteroid receptor AtBRI has GC activity in vitro. This finding may suggest that other leucine-rich receptor kinases such as the phystosulfokine receptor may also confer GC activity as it has a high degree of similarity in the domain that has been delineated as essential for catalysis. In addition, the discovery of increasing complexities in the molecular architecture of higher plant nucleotide cyclases (NCs) is entirely compatible with findings in Chlamydomonas where such domains appear in > 20 different combinations suggesting a role in highly diverse and complex signaling events.

Authors

Stuart Meier

University of the Western Cape, Bellville, South Africa

Cathal Seoighe

National Bioinformatics Network, University of Cape Town, Rondebosch, South Africa

Lusisizwe Kwezi

University of the Western Cape, Bellville, South Africa

Helen Irving

Monash University, Parkville, Melbourne, Victoria, Australia

Chris Gehring

University of the Western Cape, Bellville, South Africa

Purchase article for $19

Subscribe to this journal for $79/year