Research article summary (published 5 Jun 2005):

Molecular characterization and evolutionary study of spider tubuliform (eggcase) silk protein.

Full Abstract

As a result of hundreds of millions of years of evolution, orb-web-weaving spiders have developed the use of seven different silks produced by different abdominal glands for various functions. Tubuliform silk (eggcase silk) is unique among these spider silks due to its high serine and very low glycine content. In addition, tubuliform silk is the only silk produced just during a short period of time, the reproductive season, in the spider's life. To understand the molecular characteristics of the proteins composing this silk, we constructed tubuliform-gland-specific cDNA libraries from three different spider families, Nephila clavipes, Argiope aurantia, and Araneus gemmoides. Sequencing of tubuliform silk cDNAs reveals the repetitive architecture of its coding sequence and novel amino acid motifs. The inferred protein, tubuliform spidroin 1 (TuSp1), contains highly homogenized repeats in all three spiders. Amino acid composition comparison of the predicted tubuliform silk protein sequence to tubuliform silk indicates that TuSp1 is the major component of tubuliform silk. Repeat unit alignment of TuSp1 among three spider species shows high sequence conservation among tubuliform silk protein orthologue groups. Sequence comparison among TuSp1 repetitive units within species suggests intragenic concerted evolution, presumably through gene conversion and unequal crossover events. Comparative analysis demonstrates that TuSp1 represents a new orthologue in the spider silk gene family.

Author information

Author/s: Tian, Maozhen (M); Lewis, Randolph V (RV);

Affiliation: Department of Molecular Biology, University of Wyoming, 1000 East University Avenue, Laramie, Wyoming 82071, USA. tianmz(-atsign-)uwyo.edu

Journal and publication information

Publication Type: Comparative Study; Journal Article; Research Support, U.S. Gov't, Non-P.H.S.

Journal: Biochemistry (Biochemistry), published in United States. (Language: eng)

Reference: 2005-Jun; vol 44 (issue 22) : pp 8006-12

Dates: Created 2005/05/31; Completed 2005/08/26; Revised 2006/11/15;

PMID: 15924419, status: MEDLINE (last retrieval date: 2/18/2009, IMS Date: )

Sourced from the National Library of Medicine. Abstract text and other information may be subject to copyright.

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MeSH headings (categories)

This article was linked to the MESH Headings shown below.

Amino Acid Sequence Animals Cloning, Molecular Codon - chemistry Evolution, Molecular Female Fibroins - chemistry; genetics Gene Library Insect Proteins - chemistry; genetics

Insect Proteins - chemistry; genetics Molecular Sequence Data Repetitive Sequences, Amino Acid Sequence Analysis, DNA Sequence Analysis, Protein Sequence Homology, Amino Acid Silk - chemistry; genetics Species Specificity Spiders

Associated Chemicals: Codon (0) ; Insect Proteins (0) ; Silk (0) ; spidroin 1 (0) ; Fibroins (9007-76-5)

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