Title

HSP-70 ATPase Chaperon Protein

Poster Number

10

Format

Poster Presentation

Faculty Mentor Name

Craig Vierra

Abstract/Artist Statement

Because spider silks have extraordinary tensile strength and toughness, they have long been of interest to commercial industries that seek to harvest the durability of such fibers. However, this endeavor is only profitable if scientists are able to successfully uncover the assembly process that occurs in the silk glands. Research regarding dragline silk has been explored and specific proteins, such as MaSp 1 and MaSp2, which compose dragline silk, have been completed sequenced and these proteins have been demonstrated to be chief components of dragline silk. However, little is known about the specific proteins that assemble the silk before it is released by the black widow spider. One gene, whose expression is induced upon pulling dragline silk from black widow spiders, is the heat shock protein, HSP-70. In vertebrates HSP-70 has been demonstrated to be involved in protein folding and is induced upon chemical stress. We propose that the black widow HSP-70 may participate in the assembly of spider silk within silk glands. Recently, we isolated a partial eDNA sequence from black widow spiders that represents the spider orthologue of vertebrate HSP-70. Our eDNA sequence has identified the closest matching homolog as a heat shock protein 70 (gene HSP70) from Ambystoma mexicanum (the axolotl salamander). All proteins of the heat shock family are transcriptionally up-regulated with increased temperature. In order to further investigate the role of this gene in the production of silk fibroins in the glands of spiders, we attempted to isolate the full-length eDNA of black widow HSP-70. The research done this semester has provided verification of a more complete eDNA sequence, which can be used in further studies of the function of this heat shock protein in the process of dragline silk assembly.

Location

Wendell Phillips Center, 1st floor hallways

Start Date

3-5-2008 1:00 PM

End Date

3-5-2008 3:00 PM

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May 3rd, 1:00 PM May 3rd, 3:00 PM

HSP-70 ATPase Chaperon Protein

Wendell Phillips Center, 1st floor hallways

Because spider silks have extraordinary tensile strength and toughness, they have long been of interest to commercial industries that seek to harvest the durability of such fibers. However, this endeavor is only profitable if scientists are able to successfully uncover the assembly process that occurs in the silk glands. Research regarding dragline silk has been explored and specific proteins, such as MaSp 1 and MaSp2, which compose dragline silk, have been completed sequenced and these proteins have been demonstrated to be chief components of dragline silk. However, little is known about the specific proteins that assemble the silk before it is released by the black widow spider. One gene, whose expression is induced upon pulling dragline silk from black widow spiders, is the heat shock protein, HSP-70. In vertebrates HSP-70 has been demonstrated to be involved in protein folding and is induced upon chemical stress. We propose that the black widow HSP-70 may participate in the assembly of spider silk within silk glands. Recently, we isolated a partial eDNA sequence from black widow spiders that represents the spider orthologue of vertebrate HSP-70. Our eDNA sequence has identified the closest matching homolog as a heat shock protein 70 (gene HSP70) from Ambystoma mexicanum (the axolotl salamander). All proteins of the heat shock family are transcriptionally up-regulated with increased temperature. In order to further investigate the role of this gene in the production of silk fibroins in the glands of spiders, we attempted to isolate the full-length eDNA of black widow HSP-70. The research done this semester has provided verification of a more complete eDNA sequence, which can be used in further studies of the function of this heat shock protein in the process of dragline silk assembly.