Reflectins: The Unusual Proteins of Squid Reflective Tissues
- 9 January 2004
- journal article
- other
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 303 (5655) , 235-238
- https://doi.org/10.1126/science.1091288
Abstract
A family of unusual proteins is deposited in flat, structural platelets in reflective tissues of the squid Euprymna scolopes . These proteins, which we have named reflectins, are encoded by at least six genes in three subfamilies and have no reported homologs outside of squids. Reflectins possess five repeating domains, which are highly conserved among members of the family. The proteins have a very unusual composition, with four relatively rare residues (tyrosine, methionine, arginine, and tryptophan) comprising ∼57% of a reflectin, and several common residues (alanine, isoleucine, leucine, and lysine) occurring in none of the family members. These protein-based reflectors in squids provide a marked example of nanofabrication in animal systems.Keywords
This publication has 14 references indexed in Scilit:
- Photonic structures in biologyNature, 2003
- Cryptic coloration and mirrored sides as camouflage strategies in near‐surface pelagic habitats: Implications for foraging and predator avoidanceLimnology and Oceanography, 2003
- Cryptic and conspicuous coloration in the pelagic environmentProceedings Of The Royal Society B-Biological Sciences, 2002
- The Anatomy and Morphology of the Adult Bacterial Light Organ of Euprymna scolopes Berry (Cephalopoda:Sepiolidae)The Biological Bulletin, 1990
- Physiological color change in squid iridophoresCell and tissue research, 1990
- Physiological color change in squid iridophoresCell and tissue research, 1990
- Chromatophore Organs, Reflector Cells, Iridocytes and Leucophores in CephalopodsAmerican Zoologist, 1983
- ULTRASTRUCTURE OF A CEPHALOPOD PHOTOPHORE. II. IRIDOPHORES AS REFLECTORS AND TRANSMITTERSThe Biological Bulletin, 1974
- The physics and biology of animal reflectorsProgress in Biophysics and Molecular Biology, 1972
- Structure and molecular anisotropy of sorbic acid, CH 3 . CH : CH . CH : CH . COOHProceedings of the Royal Society of London. Series A. Mathematical and Physical Sciences, 1941