Ecological advantages from light adaptation and heterotrophic-like behavior in Synechococcus harvested from the Gulf of Trieste (Northern Adriatic Sea).
A preliminary study was carried out on a picocyanobacterial mixed culture harvested from the Gulf of Trieste (Northern Adriatic) and identified as Synechococcus spp. both by transmission electron microscopy observations, biliprotein composition and molecular analyses. Absorption and fluorescence spectra revealed phycourobilin and phycoerythrobilin chromophores, suggesting the presence of both CU- and C-phycoerythrin, besides phycocyanobilin chromophores typical for phycocyanins and allophycocyanins. Both biliprotein analyses and molecular identification indicated the presence of at least two Synechococcus subgroups presumably differing either in phycoerythrin type or in physiological traits. Among the exoenzymatic activities acting on different substrates, only aminopeptidase showed high hydrolysis rates and the uptake of organic molecules was positive for leucine but not for thymidine. The protein carbon mobilized was high compared with the leucine incorporation rates, resulting in low percentages of newly mobilized carbon utilized by cultures. The organic carbon incorporated as leucine was compared with the photosynthetically produced one, and the balance between the phototrophic- and heterotrophic-like processes was c. 3 : 1. Our findings suggest that the Synechococcus heterotrophy plays an important role in cell's metabolism, and that the photoheterotrophic behavior, together with their chromatic adaptation capability, might represent the key for the absolute dominance of this genus in the Adriatic Sea.
Paoli
Alessandro
A
Department of Biological Oceanography, National Institute of Oceanography and Experimental Geophysics, Santa Croce, Trieste, Italy. apaoli@ogs.trieste.it
Celussi
Mauro
M
Del Negro
Paola
P
Fonda Umani
Serena
S
Talarico
Laura
L
D000626:Aminopeptidases / Q000378:metabolism; D001426:Bacterial Proteins / Q000032:analysis / Q000378:metabolism; D004269:DNA, Bacterial / Q000737:chemistry / Q000235:genetics; D004275:DNA, Ribosomal / Q000737:chemistry / Q000235:genetics; D004591:Electrophoresis, Polyacrylamide Gel; D008027:Light; D008522:Mediterranean Sea; D046529:Microscopy, Electron, Transmission; D009691:Nucleic Acid Denaturation; D009930:Organic Chemicals / Q000378:metabolism*; D052980:Phycobilins / Q000032:analysis; D010798:Phycocyanin / Q000032:analysis; D010799:Phycoerythrin / Q000032:analysis; D010802:Phylogeny; D012336:RNA, Ribosomal, 16S / Q000235:genetics; D012623:Seawater / Q000382:microbiology*; D017422:Sequence Analysis, DNA; D017385:Sequence Homology; D046940:Synechococcus / Q000737:chemistry / Q000302:isolation & purification / Q000502:physiology*; D014557:Urobilin / Q000031:analogs & derivatives / Q000032:analysis
D001426:Bacterial Proteins; D004269:DNA, Bacterial; D004275:DNA, Ribosomal; D009930:Organic Chemicals; D052980:Phycobilins; D012336:RNA, Ribosomal, 16S; C002497:allophycocyanin; D010798:Phycocyanin; D010799:Phycoerythrin; C011070:phycoerythrobilin; D014557:Urobilin; C044986:phycourobilin; D000626:Aminopeptidases