Light-chain fibroin of Galleria mellonella L
Language English Country Germany Media print
Document type Journal Article, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, Non-P.H.S.
PubMed
7715595
DOI
10.1007/bf00425815
Knihovny.cz E-resources
- MeSH
- Alternative Splicing MeSH
- Bombyx genetics MeSH
- Fibroins chemistry genetics MeSH
- Insect Hormones chemistry genetics MeSH
- DNA, Complementary genetics MeSH
- Protein Conformation MeSH
- Pupa MeSH
- Larva MeSH
- RNA, Messenger metabolism MeSH
- Molecular Sequence Data MeSH
- Molecular Weight MeSH
- Moths genetics MeSH
- Poly A metabolism MeSH
- Amino Acid Sequence MeSH
- Base Sequence MeSH
- Sequence Analysis, DNA MeSH
- Sequence Homology, Amino Acid MeSH
- Sequence Homology, Nucleic Acid MeSH
- Sequence Alignment MeSH
- Animals MeSH
- Check Tag
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Research Support, U.S. Gov't, Non-P.H.S. MeSH
- Names of Substances
- Fibroins MeSH
- Insect Hormones MeSH
- DNA, Complementary MeSH
- RNA, Messenger MeSH
- Poly A MeSH
The posterior section of Galleria mellonella silk glands contains two abundant mRNAs that are identical except for the non-coding tail, which includes either two (1.1 kb mRNA) or three (1.2 kb mRNA) consensus sequences for polyadenylation sites. The transcripts are 40% homologous in the coding as well as non-coding regions with the mRNA encoding light-chain fibroin (L-fibroin) in Bombyx mori; the deduced translation product shows 43% identity with the Bombyx L-fibroin peptide, with all three cysteines conserved. Amino acid analysis of the N-termini of Galleria silk proteins revealed that L-fibroin (25 kDa) occurs in two isoforms, the shorter one lacking the Ala-Pro dipeptide residue at its N-terminus. The 29 and 30 kDa Galleria silk proteins appear to be homologs of Bombyx silk component P25. The results suggest that evolutionary diversification of Galleria and Bombyx L-fibroins involves alternative polyadenylation and proteolytic processing sites.
See more in PubMed
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Characterization and comparative analysis of sericin protein 150 in Bombyx mori
The design of silk fiber composition in moths has been conserved for more than 150 million years
GENBANK
S77817
