IMMUNOLABELING OF PHYCOERYTHRIN, RIBULOSE 1,5-BISPHOSPHATE CARBOXYLASE OXYGENASE AND NITROGENASE IN THE UNICELLULAR CYANOBIONTS OF ORNITHOCERCUS SPP (DINOPHYCEAE)

Citation
S. Janson et al., IMMUNOLABELING OF PHYCOERYTHRIN, RIBULOSE 1,5-BISPHOSPHATE CARBOXYLASE OXYGENASE AND NITROGENASE IN THE UNICELLULAR CYANOBIONTS OF ORNITHOCERCUS SPP (DINOPHYCEAE), Phycologia, 34(2), 1995, pp. 171-176
Citations number
19
Categorie Soggetti
Plant Sciences","Marine & Freshwater Biology
Journal title
ISSN journal
00318884
Volume
34
Issue
2
Year of publication
1995
Pages
171 - 176
Database
ISI
SICI code
0031-8884(1995)34:2<171:IOPR1C>2.0.ZU;2-9
Abstract
Phaeosomes, extracellular cyanobacterial symbionts of the genus Synech ococcus Nageli, of some species of tropical marine dinoflagellates wer e investigated for the presence of nitrogenase, phycoerythrin (PE) and ribulose 1,5-bisphosphate carboxylase/oxygenase (RUBISCO). The dinofl agellates Ornithocercus magnificus Stein, and O. steinii Schutt were c ollected in the Caribbean Sea, and transmission electron microscopy re vealed that, in addition to phaeosomes, bacterial consorts were also p resent between the upper and the lower girdle list of the cingular gro ove. The bacteria were uniform in size, ranging between 0.2 and 0.3 mu m approximately. Immunogold labelling techniques indicated that the c yanobacterial phaeosomes contained high amounts of the photosystem II associated pigment PE. The CO2-fixing enzyme RUBISCO was mainly locate d in carboxysomes. Those examined for nitrogenase were collected at bo th day and night, but nitrogenase was not detected. Ornithocercus spp. are non-photosynthetic organisms, and it appears that phaeosomes serv e as a carbon source for species of this genus, i.e. they have the fun ctional role of chloroplasts.