Dataset Information

Composition of minor ampullate silk makes its properties different from those of major ampullate silk

ABSTRACT: Spider’s minor ampullate silk, or MI-silk, exhibits distinct mechanical properties and water resistance compared to its major ampullate counterpart (MA-silk). The principal protein constituent of MI-silk is known as minor ampullate spidroin, or MiSp, and while its sequence has been deciphered and is thought to underlie the differences in properties with MA-silk, the composition of MI-silk and the relationship between its composition and properties remain elusive. In this study, we set out to investigate the mechanical properties, water resistance, and proteome of MA-silk and MI-silk from Araneus ventricosus and Trichonephila clavata. We also synthesized artificial fibers from major ampullate spidroin, MaSp1 and 2, and MiSp to compare their properties. Our proteomic analysis reveals that the MI-silk of both araneids is composed of MiSp, MaSp1, and spidroin constituting elements (SpiCEs). The absence of MaSp2 in the MI-silk proteome and the comparison of the water resistance of artificial fibers suggest that the presence of MaSp2 is the reason for the disparity in water resistance between MI-silk and MA-silk.

ORGANISM(S): Cellular Organisms

SUBMITTER: Kazuharu Arakawa

PROVIDER: PXD038879 | JPOST Repository | Mon Dec 18 00:00:00 GMT 2023

REPOSITORIES: jPOST

ACCESS DATA

Dataset's files

Source:

			Action	DRS
	200327mm_018_Jorogumo-%237605-U-191024-1_Chymotrypsin_200ng.d.zip	Other
	200327mm_019_Jorogumo-%237605-U-191031-1_Chymotrypsin_200ng.d.zip	Other
	200327mm_020_Jorogumo-%237626-U-191017-1_Chymotrypsin_200ng.d.zip	Other
	200327mm_021_Jorogumo-%237626-U-191018-1_Chymotrypsin_200ng.d.zip	Other
	200327mm_022_Jorogumo-%237627-U-191017-1_Chymotrypsin_200ng.d.zip	Other

Items per page:

1 - 5 of 20

Similar Datasets

Project description:Spider silk proteins are synthesized in the silk-producing glands, where the spidroins are produced, stored and processed into a solid fiber from a crystalline liquid solution. Despite great interest in the spider silk properties, that make this material suitable for biomedical and biotechnological applications, the mechanism of formation and spinning of the silk fibers has not been fully elucidated; and no combination of proteomic and transcriptomic study has been carried out so far in the spider silk-producing glands. Nephila clavipes is an attractive orb-web spider to investigate the spinning process of silk production, given the properties of strength, elasticity and biocompatibility of their silk fibers. Thus, considering that the combination of proteomic and transcriptomic analysis may reveal an extensive repertoire of novel proteins involved in the silk spinning process, and in order to facilitate and enable proteomics in this non-model organism, the current study aims to construct a high quality reference mRNA-derived protein database that could be used to identify tissue specific expression patterns in spider silk glands. Next-generation sequencing has offered a powerful and cost-efficient technique for the generation of transcriptomic datasets in non-model species using diverse platforms such as the Illumina HiSeq, Roche 454, Pacific Biosystems, and Applied Biosystems SOLiD; In the current study, the Illumina HiSeq 2000 platform will be used to generate a N. clavipes spider silk glands transcriptome-based protein database. The transcriptome data generated in this study will provide a comprehensive and valuable genomic resource for future research of the group of spider silk-producing glands, in order to improve our understanding of the overall mechanism of action involved in production, secretion, storage, transport, protection and conformational changes of spidroins during the spinning process, and prey capture; and the results may be relevant for scientists in material Science, biology, biochemistry, and environmental scientists.

Dataset Information

Composition of minor ampullate silk makes its properties different from those of major ampullate silk

Dataset's files

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure

Tweets