Chromatic adaptation in a mutant of Fremyella diplosiphon incapable of phycoerythrin synthesis.

A mutant of the chromatically adapting cyanobacterium Fremyella diplosiphon, incapable of phycoerythrin synthesis but responding to wavelength modulation of its biliprotein content, was isolated. The biliprotein composition of the mutant and of the wild type were identical after growth in red light, but green light induced, in the mutant, the synthesis of a biliviolin-type chromophore bound to some of the alpha subunits of its phycocyanin. Implications of the results on the regulation and possible pathways of biliprotein biosynthesis are discussed.

The cyanobacteriales: a legitimate order based on the type strain Cyanobacterium stanieri?

As a logical consequence of the definition of a bacterium (Stanier and van Niel, 1962), R. Y. Stanier created the name "cyanobacteria" as a replacement for "blue-green algae".

Effects of chromatic illumination on cyanobacterial phycobilisomes. Evidence for the specific induction of a second pair of phycocyanin subunits in Pseudanabaena 7409 grown in red light.

Pseudanabaena 7409 is a chromatically cyanobacterium which photocontrols the synthesis of both phycoerythrin and phycocyanin [Tandeau de Marsac (1977) J. Bacteriol. 130, 82--91].

Wavelength modulation of phycoerythrin synthesis in Synechocystis sp. 6701.

The spectral dependence of phycoerythrin synthesis has been studied in a unicellular photautotrophic cyanobacterium, Synechocystis sp. 6701, in which phycoerythrin synthesis alone is under chromatic control. Cells were partially depleted of their phycobiliprotein pigments through nitrate starvation in the light.

Molecular composition of cyanobacterial phycobilisomes.

Phycobilisomes isolated from eight different species of cyanobacteria contain in addition to the light-harvesting phycobiliproteins, a small number of colorless polypeptides with molecular weights higher than those of the chromopolypeptide subunits of the phycobiliproteins. In the phycobilisomes of the species examined, from four to nine colorless polypeptides were resolved by sodium dodecyl sulfate/polyacrylamide gel electrophoresis. Those of highest molecular weight (70,000-120,000) also occurred in the washed membrane fraction of the cell and may therefore be derived from the thylakoids, to which the phycobilisomes are attached in vivo.