A potentially useful cyanobacterial sulfated exopolysaccharide and its biosynthesis and regulation genes, which contribute to the laboratorial bloom formation, are elucidated for the first time among prokaryotes.
The structure of the photosystem I (PSI) complex from Synechocystis is determined, and reaction center subunits engineered to resemble a viral PSI are found to promote promiscuous electron acceptor properties.
Phototrophic growth laws are elucidated by combining computational modeling and experiments for quantitative evaluation of cellular physiology, morphology and proteome allocation across a wide range of light conditions.
The necessity of studying extremophile organisms is exemplified by the structure of photosystem I from a high-light tolerant cyanobacteria, demonstrating the relationship between the structure and function in photosystem I.
Carboxysomes, the carbon-fixation machinery of cyanobacteria, are equidistantly-positioned by dynamic gradients of the protein McdA on the nucleoid that emerge through interaction with a previously unidentified carboxysome factor, McdB.
The nature of the phycobilisome–photosystem II supercomplex on the native thylakoid determined with cryo-electron tomography at an unprecedented resolution reveals that one phycobilisome interconnects with six photosystem monomers.