β-Keratins in crocodiles reveal amino acid homology with avian keratins Article

Ye, C, Wu, X, Yan, P et al. (2010). β-Keratins in crocodiles reveal amino acid homology with avian keratins . MOLECULAR BIOLOGY REPORTS, 37(3), 1169-1174. 10.1007/s11033-009-9480-z

cited authors

  • Ye, C; Wu, X; Yan, P; Amato, G

authors

abstract

  • The DNA sequences encoding β-keratin have been obtained from Marsh Mugger (Crocodylus palustris) and Orinoco Crocodiles (Crocodylus intermedius). Through the deduced amino acid sequence, these proteins are rich in glycine, proline and serine. The central region of the proteins are composed of two beta-folded regions and show a high degree of identity with β-keratins of aves and squamates. This central part is thought to be the site of polymerization to build the framework of β-keratin filaments. It is believed that the β-keratins in reptiles and birds share a common ancestry. Near the C-terminal, these β-keratins contain a peptide rich in glycine-X and glycine-X-X, and the distinctive feature of the region is some 12-amino acid repeats, which are similar to the 13-amino acid repeats in chick scale keratin but absent from avian feather keratin. From our phylogenetic analysis, the β-keratins in crocodile have a closer relationship with avian keratins than the other keratins in reptiles. © Springer Science+Business Media B.V. 2009.

publication date

  • March 1, 2010

published in

Digital Object Identifier (DOI)

start page

  • 1169

end page

  • 1174

volume

  • 37

issue

  • 3