Beta-keratin explained

Beta-keratin should not be confused with beta-carotene.

Beta-keratin (β-keratin) is a member of a structural protein family found in the epidermis of reptiles and birds.[1] [2] Beta-keratins were named so because they are components of epidermal stratum corneum rich in stacked beta sheets, in contrast to alpha-keratins, intermediate-filament proteins also found in stratum corneum and rich in alpha helices.[3] Because the accurate use of the term keratin is limited to the alpha-keratins, the term "beta-keratins" in recent works is replaced by "corneous beta-proteins"[4] or "keratin-associated beta-proteins."[5]

β-keratins add much more rigidity to reptilian skin than alpha-keratins alone do to mammalian skin. β-keratins are impregnated into the stratum corneum of the reptilian skin, providing waterproofing and the prevention of desiccation.

The scales, beaks, claws and feathers of birds contain β-keratin of the avian family. Phylogenetic studies of β-keratin sequences show that feather β-keratins evolved from scale β-keratins.[6] The scale β-keratins form the basal group in avians. Duplication and divergence events then led to claw β-keratin genes, and further recombination resulted in new feather and feather-like avian β-keratin genes. Evidence for these duplication events comes from the correlation of feather β-keratin clade structure with their genomic loci.[7]

Changes in β-keratins may have also influenced the development of powered flight. A recent study using molecular dating methods to link the evolution of avian β-keratin genes in general to that of feathers specifically reveals that the avian β-keratin family began diverging from the crocodile family about 216 million years ago.[7] It also found that the feather β-keratin family did not begin diverging until 125 million years ago, a date consistent with the adaptive radiation of birds during the Cretaceous. β-keratins found in modern feathers have increased elasticity, a factor that may have contributed to their role in flight.[7] Thus, feathered relatives of birds such as Anchiornis and Archaeopteryx, whose flight capabilities have been questioned,[8] would have had avian, but not feather, β-keratins.

The small alvarezsaurid dinosaur Shuvuuia deserti shows evidence of a featherlike skin covering. Analysis by Schweitzer et al. (1999) showed that these featherlike structures consisted of beta-keratin.[9] This has since been refuted by Saitta et al., finding that the fibers analyzed instead consisted of inorganic calcium phosphate as evidenced by fluorescence under cross polarised light.[10] Signals from immunohistochemical analyses on fossil samples are prone to false positives and must be used with caution when dealing with geological samples.

Notes and References

  1. Dalla Valle L, Nardi A, Belvedere P, Toni M, Alibardi L . Beta-keratins of differentiating epidermis of snake comprise glycine-proline-serine-rich proteins with an avian-like gene organization . Dev. Dyn. . 236 . 7 . 1939–53 . July 2007 . 17576619 . 10.1002/dvdy.21202. free .
  2. Dalla Valle L, Nardi A, Toffolo V, Niero C, Toni M, Alibardi L . Cloning and characterization of scale beta-keratins in the differentiating epidermis of geckoes show they are glycine-proline-serine-rich proteins with a central motif homologous to avian beta-keratins . Dev. Dyn. . 236 . 2 . 374–88 . February 2007 . 17191254 . 10.1002/dvdy.21022. free .
  3. Calvaresi M, Eckhart L, Alibardi L . The molecular organization of the beta-sheet region in Corneous beta-proteins (beta-keratins) of sauropsids explains its stability and polymerization into filaments . J. Struct. Biol. . 194 . 3 . 282–91 . June 2016 . 26965557 . 10.1016/j.jsb.2016.03.004.
  4. Calvaresi M, Eckhart L, Alibardi L . The molecular organization of the beta-sheet region in Corneous beta-proteins (beta-keratins) of sauropsids explains its stability and polymerization into filaments . J. Struct. Biol. . 194 . 3 . 282–91 . June 2016 . 26965557 . 10.1016/j.jsb.2016.03.004.
  5. Alibardi L . Cornification in reptilian epidermis occurs through the deposition of keratin-associated beta-proteins (beta-keratins) onto a scaffold of intermediate filament keratins . J. Morphol. . 274 . 2 . 175–93 . Feb 2013 . 23065677 . 10.1002/jmor.20086. 23739887 .
  6. Greenwold. M.J.. Sawyer, R.H.. Genomic organization and molecular phylogenies of the beta (β) keratin multigene family in the chicken (Gallus gallus) and zebra finch (Taeniopygia guttata): implications for feather evolution. BMC Evolutionary Biology. 2010. 10. 10.1186/1471-2148-10-148. 148. 20482795. 2894828 . free .
  7. Greenwold. M.J.. Sawyer, R.H.. Linking the molecular evolution of avian beta (β) keratins to the evolution of feathers. Journal of Experimental Zoology. 2011. 316B. 8. 609–616. 10.1002/jez.b.21436. 21898788. 2011JEZB..316..609G .
  8. Nudds. R.L.. Dyke, G.J.. 12340187. Narrow Primary Feather Rachises in Confuciusornis and Archaeopteryx Suggest Poor Flight Ability. Science. 14 May 2010. 328. 5980. 887–889. 10.1126/science.1188895. 20466930. 2010Sci...328..887N .
  9. .Schweitzer, Mary Higby, Watt, J.A., Avci, R., Knapp, L., Chiappe, L, Norell, Mark A., Marshall, M. (1999). "Beta-Keratin Specific Immunological reactivity in Feather-Like Structures of the Cretaceous Alvarezsaurid, Shuvuuia deserti Journal of Experimental Biology (Mol Dev Evol) 255:146-157
  10. .Saitta, Evan T., Fletcher, I., Martin, P., Pittman, M., Kaye, Thomas G., True, Lawrence D., Norell, Mark A., Abbott, Geoffrey D., Summons, Roger E., Penkman, K., Vinther, J. (2018). "Preservation of feather fibers from the Late Cretaceous dinosaur Shuvuuia deserti raises concern about immunohistochemical analyses on fossils". Organic Geochemistry 125:142-151

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