C. Lichtle et al., IMMUNOLOGICAL AND ULTRASTRUCTURAL CHARACTERIZATION OF THE PHOTOSYNTHETIC COMPLEXES OF THE PROCHLOROPHYTE PROCHLOROCOCCUS (OXYCHLOROBACTERIA), Journal of phycology, 31(6), 1995, pp. 934-941
Ultrastructural features and immunological properties of some thylakoi
d proteins were examined in two strains of the prochlorophyte Prochlor
ococcus and compared to those of other photosynthetic prokaryotes and
eukaryotes. Both strains exhibited two or three rows of tightly appres
sed thylakoidal membranes, located at the cell periphery. However, thy
lakoids were concentrically arranged in the strain from the Sargasso S
ea (SARG) and horseshoe-shaped in the Mediterranean isolate (CCMP 1378
). Although backing phycobilisomes, both cell types shared with cyanob
acteria the presence of carboxysome-like structures and glycogen granu
les as storage compounds. The main thylakoid polypeptides separated by
sodium dodecyl sulfate-polyacrylamide gel electrophoresis were charac
terized by Western blotting using several antibodies. The 30-kDa polyp
eptide of the light-harvesting complex (LHC) of Prochlorococcus showed
a weak positive immunological cross-reaction with an antibody raised
against the 32-kDa apoprotein of the LHC of the prochlorophyte Prochlo
rothrix hollandica. In contrast, it showed no immunological relationsh
ips with the chlorophyll a/b (Chl a/b) LHCs of green algae and higher
plants. Protein membranes from Prochlorococcus strongly cross-reacted
with antibodies raised against reaction center polypeptides of photosy
stems II and I (PSs II and I) of other photosynthetic organisms, confi
rming the high degree of conservation of these basic compounds of the
photosynthetic machinery during evolution. Immunolocalization of thyla
koid proteins showed that the LHC proteins, the major PS II reaction c
enter proteins (CP 43 and D2), and the PS I reaction center proteins w
ere equally distributed within the thylakoid membranes in contrast to
the segregation observed in higher plants and green alga thylakoids. W
e also identified ribulose-1,5-bisphosphate carboxybase/oxygenase in t
he carboxysomes. These results suggest that Prochlorococcus is more cl
osely related to cyanobacteria than to green plastids even though in c
ontains Chl b.