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Structure and post-translational modifications of the web silk protein spidroin-1 from Nephila spiders

Title data

dos Santos-Pinto, José R. A. ; Lamprecht, Günther ; Chen, Wei-Qiang ; Heo, Seok ; Hardy, John G. ; Priewalder, Helga ; Scheibel, Thomas ; Palma, Mario Sergio ; Lubec, Gert:
Structure and post-translational modifications of the web silk protein spidroin-1 from Nephila spiders.
In: Journal of Proteomics. Vol. Vol. 105 (13 June 2014) . - pp. 174-185.
ISSN 1876-7737
DOI: https://doi.org/10.1016/j.jprot.2014.01.002

Abstract in another language

Spidroin-1 is one of the major ampullate silk proteins produced by spiders for use in the construction of the frame and radii of orb webs, and as a dragline to escape from predators. Only partial sequences of spidroin-1 produced by Nephila clavipes have been reported up to now, and there is no information on post-translational modifications (PTMs). A gel-based mass spectrometry strategy with ETD and CID fragmentation methods were used to sequence and determine the presence/location of any PTMs on the spidroin-1. Sequence coverage of 98.06%, 95.05%, and 98.37% were obtained for N. clavipes, Nephila edulis and for Nephila madagascariensis, respectively. Phosphorylation was the major PTM observed with 8 phosphorylation sites considered reliable on spidroin-1 produced by N. clavipes, 4 in N. madagascariensis and 2 for N. edulis. Dityrosine and 3,4-dihydroxyphenylalanine (formed by oxidation of the spidroin-1) were observed, although the mechanism by which they are formed (i.e. exposure to UV radiation or to peroxidases in the major ampullate silk gland) is uncertain. Herein we present structural information on the spidroin-1 produced by three different Nephila species; these findings may be valuable for understanding the physicochemical properties of the silk proteins and moreover, future designs of recombinantly produced spider silk proteins.

Biotechnological significance

The present investigation shows for the first time spidroin structure and post-translational modifications observed on the major ampullate silk spidroin-1. The many site specific phosphorylations (localized within the structural motifs) along with the probably photoinduction of hydroxylations may be relevant for scientists in material science, biology, biochemistry and environmental scientists. Up to now all the mechanical properties of the spidroin have been characterized without any consideration about the existence of PTMs in the sequence of spidroins. Thus, these findings for major ampullate silk spidroin-1 from Nephila spiders provide the basis for mechanical–elastic property studies of silk for biotechnological and biomedical potential applications. This article is part of a Special Issue entitled: Proteomics of non-model organisms.

Further data

Item Type: Article in a journal
Refereed: Yes
Keywords: Proteomic analysis; Mass spectrometry; Peptide sequencing; Phosphorylation;
Dityrosine
Institutions of the University: Faculties
Faculties > Faculty of Engineering Science
Faculties > Faculty of Engineering Science > Chair Biomaterials > Chair Biomaterials - Univ.-Prof. Dr. Thomas Scheibel
Faculties > Faculty of Engineering Science > Chair Biomaterials
Profile Fields > Advanced Fields > Advanced Materials
Profile Fields > Advanced Fields > Molecular Biosciences
Profile Fields > Advanced Fields > Polymer and Colloid Science
Profile Fields > Emerging Fields > Food and Health Sciences
Profile Fields
Profile Fields > Advanced Fields
Profile Fields > Emerging Fields
Result of work at the UBT: Yes
DDC Subjects: 600 Technology, medicine, applied sciences > 620 Engineering
Date Deposited: 02 Mar 2015 07:31
Last Modified: 09 Mar 2016 13:59
URI: https://eref.uni-bayreuth.de/id/eprint/7610