Literature DB >> 11040284

Dynamic rearrangement within the Antheraea pernyi silk fibroin gene is associated with four types of repetitive units.

H Sezutsu1, K Yukuhiro.   

Abstract

We characterized a full-length gene encoding wild silkmoth Antheraea pernyi fibroin (Ap-fibroin) to clarify the conformation of repetitive sequences. The gene consisted of a first exon encoding 14 amino acid residues, a short intron (120 bp), and a long second exon encoding 2,625 amino acid residues. Three amino acids, alanine, glycine, and serine, amounted to 81% of the Ap-fibroin sequence. The Ap-fibroin, except for 155 residues of the amino terminus, was composed of 80 tandemly arranged polyalanine-containing units (motifs). A motif was a doublet of a polyalanine block (PAB) and a nonpolyalanine block (NPAB). Seventy-eight of the 80 motifs were classified into four types based on differences in the NPAB sequences. Although respective motifs were significantly conserved, many rearrangements were observed within the second exon, i.e., the triplication of a 558-bp-long sequence and other duplication events of shorter sequences. Chi-like sequences, GCTGGAG, might contribute to the rearrangement within the gene as described in human minisatellite loci, because they were found at specific sites of NPAB-encoding sequences in three of four types of motifs. The present results support the idea that the Ap-fibroin gene is unstable like minisatellite sequences and that the evolution of this gene is strongly associated with its instability.

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Year:  2000        PMID: 11040284     DOI: 10.1007/s002390010095

Source DB:  PubMed          Journal:  J Mol Evol        ISSN: 0022-2844            Impact factor:   2.395


  21 in total

Review 1.  Elastomeric gradients: a hedge against stress concentration in marine holdfasts?

Authors:  J Herbert Waite; Eleonora Vaccaro; Chengjun Sun; Jared M Lucas
Journal:  Philos Trans R Soc Lond B Biol Sci       Date:  2002-02-28       Impact factor: 6.237

2.  Containment of extended length polymorphisms in silk proteins.

Authors:  Alberto Chinali; Wolfram Vater; Baerbel Rudakoff; Alexander Sponner; Eberhard Unger; Frank Grosse; Karl-Heinz Guehrs; Klaus Weisshart
Journal:  J Mol Evol       Date:  2010-03-27       Impact factor: 2.395

3.  The design of silk fiber composition in moths has been conserved for more than 150 million years.

Authors:  Naoyuki Yonemura; Frantisek Sehnal
Journal:  J Mol Evol       Date:  2006-06-03       Impact factor: 2.395

Review 4.  Silks produced by insect labial glands.

Authors:  Frantisek Sehnal; Tara Sutherland
Journal:  Prion       Date:  2008-10-20       Impact factor: 3.931

5.  Rapid evolution of pearl oyster shell matrix proteins with repetitive, low-complexity domains.

Authors:  Carmel McDougall; Felipe Aguilera; Bernard M Degnan
Journal:  J R Soc Interface       Date:  2013-02-20       Impact factor: 4.118

6.  Conservation of silk genes in Trichoptera and Lepidoptera.

Authors:  Naoyuki Yonemura; Kazuei Mita; Toshiki Tamura; Frantisek Sehnal
Journal:  J Mol Evol       Date:  2009-05-16       Impact factor: 2.395

7.  Molecular evolution of lepidopteran silk proteins: insights from the ghost moth, Hepialus californicus.

Authors:  Matthew A Collin; Kazuei Mita; Frantisek Sehnal; Cheryl Y Hayashi
Journal:  J Mol Evol       Date:  2010-05-11       Impact factor: 2.395

8.  Antheraea pernyi silk fiber: a potential resource for artificially biospinning spider dragline silk.

Authors:  Yaopeng Zhang; Hongxia Yang; Huili Shao; Xuechao Hu
Journal:  J Biomed Biotechnol       Date:  2010-05-05

9.  Structure of Animal Silks.

Authors:  Wenwen Zhang; Yimin Fan
Journal:  Methods Mol Biol       Date:  2021

Review 10.  Structure of Silk I (Bombyx mori Silk Fibroin before Spinning) -Type II β-Turn, Not α-Helix.

Authors:  Tetsuo Asakura
Journal:  Molecules       Date:  2021-06-17       Impact factor: 4.411

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