title: Biliprotein maturation: the chromophore attachment.
abstract: Biliproteins are a widespread group of brilliantly coloured photoreceptors characterized by linear tetrapyrrolic chromophores, bilins, which are covalently bound to the apoproteins via relatively stable thioether bonds. Covalent binding stabilizes the chromoproteins and is mandatory for phycobilisome assembly; and, it is also important in biliprotein applications such as fluorescence labelling. Covalent binding has, on the other hand, also considerably hindered biliprotein research because autocatalytic chromophore additions are rare, and information on enzymatic addition by lyases was limited to a single example, an EF-type lyase attaching phycocyanobilin to cysteine-alpha84 of C-phycocyanin. The discovery of new activities for the latter lyases, and of new types of lyases, have reinvigorated research activities in the subject. So far, work has mainly concentrated on cyanobacterial phycobiliproteins. Methodological advances in the process, however, as well as the finding of often large numbers of homologues, opens new possibilities for research on the subsequent assembly/disassembly of the phycobilisome in cyanobacteria and red algae, on the assembly and organization of the cryptophyte light-harvesting system, on applications in basic research such as protein folding, and on the use of phycobiliproteins for labelling.
authors.affiliation: Department Biologie I, Universität München, Menzinger Strasse 67, D-80638 München, Germany.
authors.forename: H
authors.initials: H
authors.lastname: Scheer
authors.forename: K-H
authors.initials: KH
authors.lastname: Zhao
mesh_terms: D001426:Bacterial Proteins / Q000378:metabolism*; D000458:Cyanobacteria / Q000502:physiology*; D052979:Phycobiliproteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D000461:Rhodophyta / Q000502:physiology*
chemical_list: D001426:Bacterial Proteins; D052979:Phycobiliproteins