TY - JOUR

T1 - Characterisation of nitric oxide synthase in three cnidarian-dinoflagellate symbioses

AU - Safavi-Hemami, Helena

AU - Young, Neil D

AU - Doyle, Jason

AU - Llewellyn, Lyndon

AU - Klueter, Anke

PY - 2010/4/28

Y1 - 2010/4/28

N2 - BACKGROUND: Nitric oxide synthase (NOS) is an enzyme catalysing the conversion of L-arginine to L-citrulline and nitric oxide (NO), the latter being an essential messenger molecule for a range of biological processes. Whilst its role in higher vertebrates is well understood little is known about the role of this enzyme in early metazoan groups. For instance, NOS-mediated signalling has been associated with Cnidaria-algal symbioses, however controversy remains about the contribution of enzyme activities by the individual partners of these mutualistic relationships.METHODOLOGY/PRINCIPAL FINDINGS: Using a modified citrulline assay we successfully measured NOS activity in three cnidarian-algal symbioses: the sea anemone Aiptasia pallida, the hard coral Acropora millepora, and the soft coral Lobophytum pauciflorum, so demonstrating a wide distribution of this enzyme in the phylum Cnidaria. Further biochemical (citrulline assay) and histochemical (NADPH-diaphorase) investigations of NOS in the host tissue of L. pauciflorum revealed the cytosolic and calcium dependent nature of this enzyme and its in situ localisation within the coral's gastrodermal tissue, the innermost layer of the body wall bearing the symbiotic algae. Interestingly, enzyme activity could not be detected in symbionts freshly isolated from the cnidarians, or in cultured algal symbionts.CONCLUSIONS/SIGNIFICANCE: These results suggest that NOS-mediated NO release may be host-derived, a finding that has the potential to further refine our understanding of signalling events in cnidarian-algal symbioses.

AB - BACKGROUND: Nitric oxide synthase (NOS) is an enzyme catalysing the conversion of L-arginine to L-citrulline and nitric oxide (NO), the latter being an essential messenger molecule for a range of biological processes. Whilst its role in higher vertebrates is well understood little is known about the role of this enzyme in early metazoan groups. For instance, NOS-mediated signalling has been associated with Cnidaria-algal symbioses, however controversy remains about the contribution of enzyme activities by the individual partners of these mutualistic relationships.METHODOLOGY/PRINCIPAL FINDINGS: Using a modified citrulline assay we successfully measured NOS activity in three cnidarian-algal symbioses: the sea anemone Aiptasia pallida, the hard coral Acropora millepora, and the soft coral Lobophytum pauciflorum, so demonstrating a wide distribution of this enzyme in the phylum Cnidaria. Further biochemical (citrulline assay) and histochemical (NADPH-diaphorase) investigations of NOS in the host tissue of L. pauciflorum revealed the cytosolic and calcium dependent nature of this enzyme and its in situ localisation within the coral's gastrodermal tissue, the innermost layer of the body wall bearing the symbiotic algae. Interestingly, enzyme activity could not be detected in symbionts freshly isolated from the cnidarians, or in cultured algal symbionts.CONCLUSIONS/SIGNIFICANCE: These results suggest that NOS-mediated NO release may be host-derived, a finding that has the potential to further refine our understanding of signalling events in cnidarian-algal symbioses.

KW - Animals

KW - Anthozoa

KW - Cnidaria/enzymology

KW - Dinoflagellida/enzymology

KW - Nitric Oxide/metabolism

KW - Nitric Oxide Synthase/analysis

KW - Sea Anemones

KW - Symbiosis

U2 - 10.1371/journal.pone.0010379

DO - 10.1371/journal.pone.0010379

M3 - Journal article

C2 - 20442851

VL - 5

SP - e10379

JO - PLoS ONE

JF - PLoS ONE

SN - 1932-6203

IS - 4

ER -