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Complete gene sequence of spider attachment silk protein (PySp1) reveals novel linker regions and extreme repeat homogenization.
Insect Biochem Mol Biol. 2017 02; 81:80-90.IB

Abstract

Spiders use a myriad of silk types for daily survival, and each silk type has a unique suite of task-specific mechanical properties. Of all spider silk types, pyriform silk is distinct because it is a combination of a dry protein fiber and wet glue. Pyriform silk fibers are coated with wet cement and extruded into "attachment discs" that adhere silks to each other and to substrates. The mechanical properties of spider silk types are linked to the primary and higher-level structures of spider silk proteins (spidroins). Spidroins are often enormous molecules (>250 kDa) and have a lengthy repetitive region that is flanked by relatively short (∼100 amino acids), non-repetitive amino- and carboxyl-terminal regions. The amino acid sequence motifs in the repetitive region vary greatly between spidroin type, while motif length and number underlie the remarkable mechanical properties of spider silk fibers. Existing knowledge of pyriform spidroins is fragmented, making it difficult to define links between the structure and function of pyriform spidroins. Here, we present the full-length sequence of the gene encoding pyriform spidroin 1 (PySp1) from the silver garden spider Argiope argentata. The predicted protein is similar to previously reported PySp1 sequences but the A. argentata PySp1 has a uniquely long and repetitive "linker", which bridges the amino-terminal and repetitive regions. Predictions of the hydrophobicity and secondary structure of A. argentata PySp1 identify regions important to protein self-assembly. Analysis of the full complement of A. argentata PySp1 repeats reveals extreme intragenic homogenization, and comparison of A. argentata PySp1 repeats with other PySp1 sequences identifies variability in two sub-repetitive expansion regions. Overall, the full-length A. argentata PySp1 sequence provides new evidence for understanding how pyriform spidroins contribute to the properties of pyriform silk fibers.

Authors+Show Affiliations

Department of Biology, University of California, Riverside, 900 University Ave., Riverside, 92521 CA, USA. Electronic address: ro.chaw@ucr.edu.Clemson University Genomics and Computational Biology Facility, Institute for Translational Genomics, Biosystems Research Complex #310, 105 Collings St., Clemson, 29634 SC, USA. Electronic address: saski@clemson.edu.Department of Biology, University of California, Riverside, 900 University Ave., Riverside, 92521 CA, USA; Division of Invertebrate Zoology, American Museum of Natural History, Central Park West at 79th Street, New York, NY 10024, USA. Electronic address: cheryl.hayashi@ucr.edu.

Pub Type(s)

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

Language

eng

PubMed ID

28057598

Citation

Chaw, Ro Crystal, et al. "Complete Gene Sequence of Spider Attachment Silk Protein (PySp1) Reveals Novel Linker Regions and Extreme Repeat Homogenization." Insect Biochemistry and Molecular Biology, vol. 81, 2017, pp. 80-90.
Chaw RC, Saski CA, Hayashi CY. Complete gene sequence of spider attachment silk protein (PySp1) reveals novel linker regions and extreme repeat homogenization. Insect Biochem Mol Biol. 2017;81:80-90.
Chaw, R. C., Saski, C. A., & Hayashi, C. Y. (2017). Complete gene sequence of spider attachment silk protein (PySp1) reveals novel linker regions and extreme repeat homogenization. Insect Biochemistry and Molecular Biology, 81, 80-90. https://doi.org/10.1016/j.ibmb.2017.01.002
Chaw RC, Saski CA, Hayashi CY. Complete Gene Sequence of Spider Attachment Silk Protein (PySp1) Reveals Novel Linker Regions and Extreme Repeat Homogenization. Insect Biochem Mol Biol. 2017;81:80-90. PubMed PMID: 28057598.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Complete gene sequence of spider attachment silk protein (PySp1) reveals novel linker regions and extreme repeat homogenization. AU - Chaw,Ro Crystal, AU - Saski,Christopher A, AU - Hayashi,Cheryl Y, Y1 - 2017/01/02/ PY - 2016/11/26/received PY - 2016/12/27/revised PY - 2017/01/01/accepted PY - 2017/1/7/pubmed PY - 2017/8/29/medline PY - 2017/1/7/entrez KW - Argiope argentata KW - Intragenic homogenization KW - Linker KW - Pyriform silk SP - 80 EP - 90 JF - Insect biochemistry and molecular biology JO - Insect Biochem. Mol. Biol. VL - 81 N2 - Spiders use a myriad of silk types for daily survival, and each silk type has a unique suite of task-specific mechanical properties. Of all spider silk types, pyriform silk is distinct because it is a combination of a dry protein fiber and wet glue. Pyriform silk fibers are coated with wet cement and extruded into "attachment discs" that adhere silks to each other and to substrates. The mechanical properties of spider silk types are linked to the primary and higher-level structures of spider silk proteins (spidroins). Spidroins are often enormous molecules (>250 kDa) and have a lengthy repetitive region that is flanked by relatively short (∼100 amino acids), non-repetitive amino- and carboxyl-terminal regions. The amino acid sequence motifs in the repetitive region vary greatly between spidroin type, while motif length and number underlie the remarkable mechanical properties of spider silk fibers. Existing knowledge of pyriform spidroins is fragmented, making it difficult to define links between the structure and function of pyriform spidroins. Here, we present the full-length sequence of the gene encoding pyriform spidroin 1 (PySp1) from the silver garden spider Argiope argentata. The predicted protein is similar to previously reported PySp1 sequences but the A. argentata PySp1 has a uniquely long and repetitive "linker", which bridges the amino-terminal and repetitive regions. Predictions of the hydrophobicity and secondary structure of A. argentata PySp1 identify regions important to protein self-assembly. Analysis of the full complement of A. argentata PySp1 repeats reveals extreme intragenic homogenization, and comparison of A. argentata PySp1 repeats with other PySp1 sequences identifies variability in two sub-repetitive expansion regions. Overall, the full-length A. argentata PySp1 sequence provides new evidence for understanding how pyriform spidroins contribute to the properties of pyriform silk fibers. SN - 1879-0240 UR - https://www.unboundmedicine.com/medline/citation/28057598/Complete_gene_sequence_of_spider_attachment_silk_protein__PySp1__reveals_novel_linker_regions_and_extreme_repeat_homogenization_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0965-1748(17)30002-4 DB - PRIME DP - Unbound Medicine ER -