A putative photoreceptor gene, TepixJ, of a thermophilic cyanobacterium is homologous to SypixJ1 that mediates positive phototaxis in the unicellular motile cyanobacterium Synechocystis sp. PCC 6803. The putative chromophore-binding GAF domain of TePixJ protein was overexpressed as a fusion with a polyhistidine tag (His-TePixJ_GAF) in Synechocystis cells and isolated to homogeneity. The photoreversible conversion of His-TePixJ_GAF showed peaks at 531, 341 and 266 nm for the green light-absorbing form (Pg form), and peaks at 433 and 287 nm for the blue light-absorbing form (Pb form). At 77K, the Pg form fluoresced at 580 nm, while the Pb form did not emit any fluorescence. Mass spectrometry of the tryptic chromopeptide demonstrated that a phycocyanobilin isomer binds to the conserved cysteine at ring A via a thioether bond. It is established that TePixJ and SyPixJ1 are novel photoreceptors in cyanobacteria ('cyanobacteriochromes') that are similar, but distinct from the phytochromes and bacteriophytochromes.

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A thermophilic cyanobacterium, Thermosynechococcus vulcanus RKN, exhibits cell aggregation under low temperature illuminated conditions as a means of physiological acclimation to avoid excess light stress. The cell aggregation was dispersed with cellulase treatment. We developed a method to quantify small amounts of cellulose by partial cellulose purification followed by quantitation of liberated glucose by cellulase. Under low temperature illuminated light conditions, cellulose accumulation was induced approximately 2-fold, to 10 μg (4 × 10(9) cells)(-1), and slightly preceded aggregation. Based on sequence similarity, three candidate genes for cellulose synthase (Tvtll0007, Tvtlr1795 and Tvtlr1930-33) were cloned from T. vulcanus. Gene disruption analysis showed that only Tvtll0007 was responsible for both the light- and low temperature-induced cell aggregation and the induction of cellulose accumulation. Gene expression analysis suggested that the low temperature illuminated conditions quickly induced expression of Tvtlr1795 and Tvtlr1930-33, while the induction of Tvtll0007 was slow. These results suggest that Tvtll0007 encodes a functional cellulose synthase whose activity may not be regulated at the transcriptional level.