title: Molecular architecture and evolution of a modular spider silk protein gene.
abstract: Spider flagelliform silk is one of the most elastic natural materials known. Extensive sequencing of spider silk genes has shown that the exons and introns of the flagelliform gene underwent intragenic concerted evolution. The intron sequences are more homogenized within a species than are the exons. This pattern can be explained by extreme mutation and recombination pressures on the internally repetitive exons. The iterated sequences within exons encode protein structures that are critical to the function of silks. Therefore, attributes that make silks exceptional biomaterials may also hinder the fixation of optimally adapted protein sequences.
authors.affiliation: Department of Molecular Biology, University of Wyoming, Laramie, WY 82071-3944, USA. hayashi@uwyo.edu
authors.forename: C Y
authors.initials: CY
authors.lastname: Hayashi
authors.forename: R V
authors.initials: RV
authors.lastname: Lewis
mesh_terms: D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003434:Crossing Over, Genetic; D004247:DNA / Q000235:genetics; D004261:DNA Replication; D019143:Evolution, Molecular; D005091:Exons; D005785:Gene Conversion; D005796:Genes; D007438:Introns; D008969:Molecular Sequence Data; D009154:Mutation; D011506:Proteins / Q000737:chemistry / Q000235:genetics*; D011995:Recombination, Genetic; D012091:Repetitive Sequences, Nucleic Acid; D012641:Selection, Genetic; D013045:Species Specificity; D013112:Spiders / Q000235:genetics*
chemical_list: C404864:FLAG protein, Nephila; D011506:Proteins; D004247:DNA