INTRACELLULAR CYANOBIONT RICHELIA-INTRACELLULARIS - ULTRASTRUCTURE AND IMMUNO-LOCALIZATION OF PHYCOERYTHRIN, NITROGENASE, RUBISCO AND GLUTAMINE-SYNTHETASE
S. Janson et al., INTRACELLULAR CYANOBIONT RICHELIA-INTRACELLULARIS - ULTRASTRUCTURE AND IMMUNO-LOCALIZATION OF PHYCOERYTHRIN, NITROGENASE, RUBISCO AND GLUTAMINE-SYNTHETASE, Marine Biology, 124(1), 1995, pp. 1-8
In marine tropical or subtropical plankton the filamentous, heterocyst
-forming cyanobacterium Richelia intracellularis forms a symbiosis wit
h the diatom Rhizosolenia clevei. An ultrastructural analysis of the a
pex of Rhizosolenia clevei showed that the cytoplasm in that particula
r part of the cell was present only where the cyanobiont was located.
The cyanobiont was, however, always outside the host cytoplasm. Vegeta
tive cells as well as the heterocysts of the cyanobiont were devoid of
gas vesicles and cyanophycin granules, while carboxysomes and large g
lycogen granules were common. The cyanobacterial cell wall apparently
remained intact in both vegetative and heterocyst cells. In green exci
tation light the heterocysts and vegetative cells emitted a bright yel
low fluorescence, indicating that both cell types possessed high conce
ntrations of the pigment phycoerythrin (PE) commonly associated with p
hotosystem (PS) II. The presence of this pigment in both cell types wa
s verified by immunogold localisation. Using the same technique, the n
itrogenase (dinitrogenase reductase) enzyme was shown to be exclusivel
y present in the heterocysts, while Rubisco was localised primarily to
the carboxysomes, which were only detected in vegetative cells. Using
an antiserum against the ammonia assimilating enzyme glutamine synthe
tase (GS), we could demonstrate very low levels of this enzyme, indica
ting repression of GS in the cyanobiont.