Correlation between fibroin amino acid sequence and physical silk properties
Language English Country United States Media print-electronic
Document type Comparative Study, Journal Article, Research Support, Non-U.S. Gov't
PubMed
12816957
DOI
10.1074/jbc.m305304200
PII: S0021-9258(20)83584-4
Knihovny.cz E-resources
- MeSH
- DNA Primers MeSH
- Fibroins chemistry genetics MeSH
- Silk MeSH
- Insect Proteins chemistry genetics MeSH
- Codon genetics MeSH
- Conserved Sequence MeSH
- Stress, Mechanical MeSH
- Molecular Sequence Data MeSH
- Moths MeSH
- Polymerase Chain Reaction MeSH
- Repetitive Sequences, Amino Acid MeSH
- Amino Acid Sequence MeSH
- Base Sequence MeSH
- Animals MeSH
- Check Tag
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Comparative Study MeSH
- Names of Substances
- DNA Primers MeSH
- Fibroins MeSH
- Silk MeSH
- Insect Proteins MeSH
- Codon MeSH
The fiber properties of lepidopteran silk depend on the amino acid repeats that interact during H-fibroin polymerization. The aim of our research was to relate repeat composition to insect biology and fiber strength. Representative regions of the H-fibroin genes were sequenced and analyzed in three pyralid species: wax moth (Galleria mellonella), European flour moth (Ephestia kuehniella), and Indian meal moth (Plodia interpunctella). The amino acid repeats are species-specific, evidently a diversification of an ancestral region of 43 residues, and include three types of regularly dispersed motifs: modifications of GSSAASAA sequence, stretches of tripeptides GXZ where X and Z represent bulky residues, and sequences similar to PVIVIEE. No concatenations of GX dipeptide or alanine, which are typical for Bombyx silkworms and Antheraea silk moths, respectively, were found. Despite different repeat structure, the silks of G. mellonella and E. kuehniella exhibit similar tensile strength as the Bombyx and Antheraea silks. We suggest that in these latter two species, variations in the repeat length obstruct repeat alignment, but sufficiently long stretches of iterated residues get superposed to interact. In the pyralid H-fibroins, interactions of the widely separated and diverse motifs depend on the precision of repeat matching; silk is strong in G. mellonella and E. kuehniella, with 2-3 types of long homogeneous repeats, and nearly 10 times weaker in P. interpunctella, with seven types of shorter erratic repeats. The high proportion of large amino acids in the H-fibroin of pyralids has probably evolved in connection with the spinning habit of caterpillars that live in protective silk tubes and spin continuously, enlarging the tubes on one end and partly devouring the other one. The silk serves as a depot of energetically rich and essential amino acids that may be scarce in the diet.
References provided by Crossref.org
Using the multi-omics approach to reveal the silk composition in Plectrocnemia conspersa
Silks produced by insect labial glands
The design of silk fiber composition in moths has been conserved for more than 150 million years
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