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Molecular characterization and evolutionary study of spider tubuliform (eggcase) silk protein.
Biochemistry 2005; 44(22):8006-12B

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.

Authors+Show Affiliations

Department of Molecular Biology, University of Wyoming, 1000 East University Avenue, Laramie, Wyoming 82071, USA. tianmz@uwyo.eduNo affiliation info available

Pub Type(s)

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

Language

eng

PubMed ID

15924419

Citation

Tian, Maozhen, and Randolph V. Lewis. "Molecular Characterization and Evolutionary Study of Spider Tubuliform (eggcase) Silk Protein." Biochemistry, vol. 44, no. 22, 2005, pp. 8006-12.
Tian M, Lewis RV. Molecular characterization and evolutionary study of spider tubuliform (eggcase) silk protein. Biochemistry. 2005;44(22):8006-12.
Tian, M., & Lewis, R. V. (2005). Molecular characterization and evolutionary study of spider tubuliform (eggcase) silk protein. Biochemistry, 44(22), pp. 8006-12.
Tian M, Lewis RV. Molecular Characterization and Evolutionary Study of Spider Tubuliform (eggcase) Silk Protein. Biochemistry. 2005 Jun 7;44(22):8006-12. PubMed PMID: 15924419.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Molecular characterization and evolutionary study of spider tubuliform (eggcase) silk protein. AU - Tian,Maozhen, AU - Lewis,Randolph V, PY - 2005/6/1/pubmed PY - 2005/8/27/medline PY - 2005/6/1/entrez SP - 8006 EP - 12 JF - Biochemistry JO - Biochemistry VL - 44 IS - 22 N2 - 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. SN - 0006-2960 UR - https://www.unboundmedicine.com/medline/citation/15924419/Molecular_characterization_and_evolutionary_study_of_spider_tubuliform__eggcase__silk_protein_ L2 - https://dx.doi.org/10.1021/bi050366u DB - PRIME DP - Unbound Medicine ER -