MARECHIARA-phytoplankton long-term time-series (1984-2006) at the fixed coastal station in the Gulf of Naples, Southern Tyrrhenian Sea

The "MARECHIARA-phytoplankton" dataset contains phytoplankton data collected in the ongoing time-series at Stn MC ( 40°48.5' N, 14°15' E) in the Gulf of Naples. This dataset spans over the period 1984-2006 and contains data of phytoplankton species composition and abundance. Phytoplankton sampling was regularly conducted from January 1984 till July 1991 and in 1995-2006. Sampling was interrupted from August 1991 till January 1995. The sampling frequency was fortnightly till 1991 and weekly since 1995. Phytoplankton samples were collected at 0.5 m depth using Niskin bottles and immediately fixed with formaldehyde (0.8-1.6% final concentration) for species identification and counts.

Chlorophyll and carotenoid binding in a simple red algal light-harvesting complex crosses phylogenetic lines

The membrane proteins of peripheral light-harvesting complexes (LHCs) bind chlorophylls and carotenoids and transfer energy to the reaction centers for photosynthesis. LHCs of chlorophytes, chromophytes, dinophytes, and rhodophytes are similar in that they have three transmembrane regions and several highly conserved Chl-binding residues. All LHCs bind Chl a, but in specific taxa certain characteristic pigments accompany Chl a: Chl b and lutein in chlorophytes, Chl c and fucoxanthin in chromophytes, Chl c and peridinin in dinophytes, and zeaxanthin in rhodophytes. The specificity of pigment binding was examined by in vitro reconstitution of various pigments with a simple light-harvesting protein (LHCaR1), from a red alga (Porphyridium cruentum), that normally has eight Chl a and four zeaxanthin molecules. The pigments typical of a chlorophyte (Spinacea oleracea), a chromophyte (Thallasiosira fluviatilis), and a dinophyte (Prorocentrum micans) were found to functionally bind to this protein as evidenced by their participation in energy transfer to Chl a, the terminal pigment. This is a demonstration of a functional relatedness of rhodophyte and higher plant LHCs. The results suggest that eight Chl-binding sites per polypeptide are an ancestral trait, and that the flexibility to bind various Chl and carotenoid pigments may have been retained throughout the evolution of LHCs.