Characterization of two closely related α-amylase paralogs in the bark beetle, Ips typographus (L.)
Language English Country United States Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
21638308
DOI
10.1002/arch.20433
Knihovny.cz E-resources
- MeSH
- alpha-Amylases genetics metabolism MeSH
- Coleoptera enzymology genetics MeSH
- Electrophoresis, Starch Gel MeSH
- Electrophoresis, Polyacrylamide Gel MeSH
- Phylogeny MeSH
- Insect Proteins genetics metabolism MeSH
- Isoenzymes genetics metabolism MeSH
- Cloning, Molecular MeSH
- RNA, Messenger metabolism MeSH
- Molecular Sequence Data MeSH
- Amino Acid Sequence MeSH
- Base Sequence MeSH
- Sequence Homology, Amino Acid * MeSH
- Animals MeSH
- Check Tag
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- alpha-Amylases MeSH
- Insect Proteins MeSH
- Isoenzymes MeSH
- RNA, Messenger MeSH
Ips typographus (L.), the eight-spined spruce bark beetle, causes severe damage throughout Eurasian spruce forests and suitable nuclear markers are needed in order to study its population structure on a genetic level. Two closely related genes encoding α-amylase in I. typographus were characterized and named AmyA and AmyB. Both α-amylase paralogs consisted of six exons and five introns. AmyA encodes a polypeptide of 483 amino acids, whereas AmyB has two alternative transcripts encoding polypeptides of 483 and 370 amino acids. The expression levels of both genes were high during larval stage and adulthood. The AmyB transcripts were absent in the pupal stage. A modification of the allozyme staining method allowed us to detect two clusters of bands on the electrophoretic gel that may correspond to the two α-amylase genes. There was a correlation between the lack of AmyB expression in pupa and the absence of the fast migrating isozyme cluster at this stage, suggesting that the faster migrating isoforms are products of the AmyB gene, whereas the slowly migrating bands are derived from the AmyA.
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