Analysis of antifreeze proteins within spruce budworm sister species

Spruce budworm (Choristoneura) species survive sub‐zero winter temperatures by producing antifreeze proteins (AFPs) encoded by a multigene family of short and long isoforms. We report in this study the first analysis of antifreeze proteins from related Choristoneura sister species. The additional th...

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Bibliographic Details
Published in:Insect molecular biology 2005-06, Vol.14 (3), p.319-326
Main Authors: Tyshenko, M.G, Doucet, D, Walker, V.K
Format: Article
Language:English
Subjects:
amino acid motifs
Amino Acid Sequence
amino acid sequences
Animals
antifreeze protein
Antifreeze Proteins - chemistry
Antifreeze Proteins - genetics
beta-helix
beta-helix structure
Choristoneura
cold tolerance
Consensus Sequence
conserved sequences
Freezing
insect proteins
Insect Proteins - chemistry
Insect Proteins - genetics
Models, Molecular
molecular evolution
Molecular Sequence Data
Moths - chemistry
Moths - genetics
multigene family
overwintering
Phylogeny
Protein Conformation
Protein Isoforms
protein structure
Seasons
sequence analysis
Species Specificity
spruce budworm
Tortricidae
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Summary:Spruce budworm (Choristoneura) species survive sub‐zero winter temperatures by producing antifreeze proteins (AFPs) encoded by a multigene family of short and long isoforms. We report in this study the first analysis of antifreeze proteins from related Choristoneura sister species. The additional thirty amino acid insert found in the longer AFP isoforms maintains the proteins beta‐helix and original fifteen amino acid (Thr‐X‐Thr) repeat motif. Analysis of the beta‐helix region shows more divergent residues surround the conserved Thr residues. Maintaining the beta‐helix structure and conserved Thr residues appear to be paramount for AFP function and surviving sub‐zero winter temperatures. Two other species within the same lepidopteran clade, Ditrysia, do not appear to contain any AFP‐like sequences.
ISSN:0962-1075
1365-2583
DOI:10.1111/j.1365-2583.2005.00562.x