Phylogenetic distribution, structural analysis and interaction of nucleotide excision repair proteins in cyanobacteria

The Radiant World of Cyanobacterial Phycobiliproteins: Examining Their Structure, Functions, and Biomedical Potentials

“…Based on their location and functional characteristics, the linker polypeptides are divided into four groups. PBS: Group I consists of L R polypeptides (27)(28)(29)(30)(31)(32)(33)(34)(35) involved in the peripheral rod assembly, together with a small number of 10 kDa rod linker polypeptides (LR 10 , LR 33 , and LR 35 , for example, which connect trimeric or hexameric PC/PE structural components into rod segments); Group II L RC polypeptides, which are between 25 and 27 kDa, take part in establishing the peripheral rods to the core subunits; LC polypeptides (8 kDa) belonging to Group III are essential for joining core components and ensuring their functional properties; and the main terminal energy emitter for PSII is Group IV, LCM (70-120 kDa), with a greater molecular weight of polypeptides that connects PBS to the photosynthetic membrane [31]. Six conserved domains (N-terminus) in rod linker polypeptides have been recognized by structural motif analysis as being crucial for the packing and assembly of rod discs into hexamers (Figure 3).…”

“…Particularly, the effects of oxidative stress can destroy DNA and result in apoptosis or mutagenesis. Both PC and PCB have been demonstrated to be effective at scavenging peroxynitrite and prohibiting damage to DNA [35]. According to Strasky et al [36], phycocyanobilins have structural similarities with the human bile pigments biliverdin and bilirubin, the former of which serves as the most effective endogenous antioxidant substrate.…”