Major ampullate spidroins from Euprosthenops australis: multiplicity at protein, mRNA and gene levels

Spider dragline silk possesses extraordinary mechanical properties. It consists of large fibrous proteins called spidroins that display modular structures. It is known to consist of two proteins: the major ampullate spidroin (MaSp) 1 and MaSp2. This study analyses MaSp sequences from the nursery-web...

Full description

Saved in:
Bibliographic Details
Published in:Insect molecular biology 2007-10, Vol.16 (5), p.551-561
Main Authors: Rising, A, Johansson, J, Larson, G, Bongcam-Rudloff, E, Engström, W, Hjälm, G
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Araneae
Base Composition
Biologi
Biology
DNA, Complementary
Euprosthenops
evolution
Fibroins - chemistry
Fibroins - genetics
major ampullate spidroin
MaSp
Medicin och hälsovetenskap
Molecular Sequence Data
Multigene Family
NATURAL SCIENCES
NATURVETENSKAP
Protein Structure, Tertiary
RNA, Messenger
Sequence Analysis, DNA
silk
spider
Spiders - genetics
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Spider dragline silk possesses extraordinary mechanical properties. It consists of large fibrous proteins called spidroins that display modular structures. It is known to consist of two proteins: the major ampullate spidroin (MaSp) 1 and MaSp2. This study analyses MaSp sequences from the nursery-web spider Euprosthenops australis. We have identified a previously uncharacterized MaSp2 sequence and a new MaSp-like spidroin, which display distinct homogenous submotifs within their respective Gly-rich repeats. Furthermore, a group of MaSp1 cDNA clones show unexpected heterogeneity. Genomic PCR identified several MaSp1 gene variants within individual spiders, which suggests the presence of a gene cluster in E. australis. Finally, the evolution of spidroin genes is discussed in relation to phylogenetic analysis of nonrepetitive C-terminal domains from diverse species.
ISSN:0962-1075
1365-2583
1365-2583
DOI:10.1111/j.1365-2583.2007.00749.x