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Full-Text Articles in Life Sciences
Cyanolyase: A Database Of Phycobilin Lyase Sequences, Motifs And Functions, Wendy M. Schluchter, Anthony Bretaudeau, Francois Coste, Florian Humily, Laurence Garczarek, Gildas Le Corguille, Christophe Six, Morgane Ratin, Olivier Collin, Frederic Partensky
Cyanolyase: A Database Of Phycobilin Lyase Sequences, Motifs And Functions, Wendy M. Schluchter, Anthony Bretaudeau, Francois Coste, Florian Humily, Laurence Garczarek, Gildas Le Corguille, Christophe Six, Morgane Ratin, Olivier Collin, Frederic Partensky
Biological Sciences Faculty Publications
CyanoLyase (http://cyanolyase.genouest.org/) is a manually curated sequence and motif database of phycobilin lyases and related proteins. These enzymes catalyze the covalent ligation of chromophores (phycobilins) to specific binding sites of phycobiliproteins (PBPs). The latter constitute the building bricks of phycobilisomes, the major light-harvesting systems of cyanobacteria and red algae. Phycobilin lyases sequences are poorly annotated in public databases. Sequences included in CyanoLyase were retrieved from all available genomes of these organisms and a few others by similarity searches using biochemically characterized enzyme sequences and then classified into 3 clans and 32 families. Amino acid motifs were computed for each family …
Phycoerythrin-Specific Bilin Lyase-Isomerase Controls Blue-Green Chromatic Acclimation In Marine Synechococcus, Wendy M. Schluchter, Avijit Biswas, Frédéric Partensky, J. A. Karty, Laurence Garczarek, A. Gutu, David M. Kehoe, A. Shukla, N. Blot, L. A. Hammad
Phycoerythrin-Specific Bilin Lyase-Isomerase Controls Blue-Green Chromatic Acclimation In Marine Synechococcus, Wendy M. Schluchter, Avijit Biswas, Frédéric Partensky, J. A. Karty, Laurence Garczarek, A. Gutu, David M. Kehoe, A. Shukla, N. Blot, L. A. Hammad
Biological Sciences Faculty Publications
The marine cyanobacterium Synechococcus is the second most abundant phytoplanktonic organism in the world's oceans. The ubiquity of this genus is in large part due to its use of a diverse set of photosynthetic light-harvesting pigments called phycobiliproteins, which allow it to efficiently exploit a wide range of light colors. Here we uncover a pivotal molecular mechanism underpinning a widespread response among marine Synechococcus cells known as type IV chromatic acclimation (CA4). During this process, the pigmentation of the two main phycobiliproteins of this organism, phycoerythrins I and II, is reversibly modified to match changes in the ambient light color …