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Tuesday, September 12, 2017

Natural GMOs Part 264. Cuttlefish may get their colour from a mobile bacterial gene.


Highlights
•Reflectin may have originated from a transposon in symbiotic Vibrio fischeri
•Reflectin can self-assemble as symmetrical building blocks for diverse reflectors
•Higher-order assembly of reflectin is triggered mainly by aromatic interaction
•The capacity for reflectin assembly originated from the protopeptid

Summary
Cephalopods, the group of animals including octopus, squid, and cuttlefish, have remarkable ability to instantly modulate body coloration and patterns so as to blend into surrounding environments or send warning signals to other animals. Reflectin is expressed exclusively in cephalopods, filling the lamellae of intracellular Bragg reflectors that exhibit dynamic iridescence and structural color change. Here, we trace the possible origin of the reflectin gene back to a transposon from the symbiotic bioluminescent bacterium Vibrio fischeri and report the hierarchical structural architecture of reflectin protein. Intrinsic self-assembly, and higher-order assembly tightly modulated by aromatic compounds, provide insights into the formation of multilayer reflectors in iridophores and spherical microparticles in leucophores and may form the basis of structural color change in cephalopods. Self-assembly and higher-order assembly in reflectin originated from a core repeating octapeptide (here named protopeptide), which may be from the same symbiotic bacteria. The origin of the reflectin gene and assembly features of reflectin protein are of considerable biological interest. The hierarchical structural architecture of reflectin and its domain and protopeptide not only provide insights for bioinspired photonic materials but also serve as unique “assembly tags” and feasible molecular platforms in biotechnology.

Keywords:cephalopods, structural color, iridescence, reflectin, origin, horizontal gene transfer, self-assembly, higher-order assembly

Origin of the Reflectin Gene and Hierarchical Assembly of Its Protein: Current Biology:




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