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Araneoid egg case silk: a fibroin with novel ensemble repeat units from the black widow spider, Latrodectus hesperus.
Biochemistry 2005; 44(30):10020-7B

Abstract

Araneoid spiders use specialized abdominal glands to manufacture up to seven different protein-based silks/glues that have diverse physical properties. The fibroin sequences that encode egg case fibers (cover silk for the egg case sac) and the secondary structure of these threads have not been previously determined. In this study, MALDI tandem TOF mass spectrometry (MS/MS) and reverse genetics were used to isolate the first egg case fibroin, named tubuliform spidroin 1 (TuSp1), from the black widow spider, Latrodectus hesperus. Real-time quantitative PCR analysis demonstrates TuSp1 is selectively expressed in the tubuliform gland. Analysis of the amino acid composition of raw egg case silk closely aligns with the predicted amino acid composition from the primary sequence of TuSp1, which supports the assertion that TuSp1 represents a major component of egg case fibers. TuSp1 is composed of highly homogeneous repeats that are 184 amino acids in length. The long stretches of polyalanine and glycine-alanine subrepeats, which account for the crystalline regions of minor ampullate and major ampullate fibers, are very poorly represented in TuSp1. However, polyserine blocks and short polyalanine stretches were highly iterated within the primary sequence, and (13)C NMR spectroscopy demonstrated that the majority of alanine was found in a beta-sheet structure in post-spun egg case silk. The TuSp1 repeat unit does not display substantial sequence similarity to any previously described fibroin genes or proteins, suggesting that TuSp1 is a highly divergent member of the spider silk gene family.

Authors+Show Affiliations

Department of Chemistry, University of the Pacific, Stockton, California 95211, USA.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

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

Language

eng

PubMed ID

16042378

Citation

Hu, Xiaoyi, et al. "Araneoid Egg Case Silk: a Fibroin With Novel Ensemble Repeat Units From the Black Widow Spider, Latrodectus Hesperus." Biochemistry, vol. 44, no. 30, 2005, pp. 10020-7.
Hu X, Lawrence B, Kohler K, et al. Araneoid egg case silk: a fibroin with novel ensemble repeat units from the black widow spider, Latrodectus hesperus. Biochemistry. 2005;44(30):10020-7.
Hu, X., Lawrence, B., Kohler, K., Falick, A. M., Moore, A. M., McMullen, E., ... Vierra, C. (2005). Araneoid egg case silk: a fibroin with novel ensemble repeat units from the black widow spider, Latrodectus hesperus. Biochemistry, 44(30), pp. 10020-7.
Hu X, et al. Araneoid Egg Case Silk: a Fibroin With Novel Ensemble Repeat Units From the Black Widow Spider, Latrodectus Hesperus. Biochemistry. 2005 Aug 2;44(30):10020-7. PubMed PMID: 16042378.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Araneoid egg case silk: a fibroin with novel ensemble repeat units from the black widow spider, Latrodectus hesperus. AU - Hu,Xiaoyi, AU - Lawrence,Barbara, AU - Kohler,Kristin, AU - Falick,Arnold M, AU - Moore,Anne M F, AU - McMullen,Erin, AU - Jones,Patrick R, AU - Vierra,Craig, PY - 2005/7/27/pubmed PY - 2005/11/8/medline PY - 2005/7/27/entrez SP - 10020 EP - 7 JF - Biochemistry JO - Biochemistry VL - 44 IS - 30 N2 - Araneoid spiders use specialized abdominal glands to manufacture up to seven different protein-based silks/glues that have diverse physical properties. The fibroin sequences that encode egg case fibers (cover silk for the egg case sac) and the secondary structure of these threads have not been previously determined. In this study, MALDI tandem TOF mass spectrometry (MS/MS) and reverse genetics were used to isolate the first egg case fibroin, named tubuliform spidroin 1 (TuSp1), from the black widow spider, Latrodectus hesperus. Real-time quantitative PCR analysis demonstrates TuSp1 is selectively expressed in the tubuliform gland. Analysis of the amino acid composition of raw egg case silk closely aligns with the predicted amino acid composition from the primary sequence of TuSp1, which supports the assertion that TuSp1 represents a major component of egg case fibers. TuSp1 is composed of highly homogeneous repeats that are 184 amino acids in length. The long stretches of polyalanine and glycine-alanine subrepeats, which account for the crystalline regions of minor ampullate and major ampullate fibers, are very poorly represented in TuSp1. However, polyserine blocks and short polyalanine stretches were highly iterated within the primary sequence, and (13)C NMR spectroscopy demonstrated that the majority of alanine was found in a beta-sheet structure in post-spun egg case silk. The TuSp1 repeat unit does not display substantial sequence similarity to any previously described fibroin genes or proteins, suggesting that TuSp1 is a highly divergent member of the spider silk gene family. SN - 0006-2960 UR - https://www.unboundmedicine.com/medline/citation/16042378/Araneoid_egg_case_silk:_a_fibroin_with_novel_ensemble_repeat_units_from_the_black_widow_spider_Latrodectus_hesperus_ L2 - https://dx.doi.org/10.1021/bi050494i DB - PRIME DP - Unbound Medicine ER -