Differential expression of two small Hsps during diapause in the corn stalk borer Sesamia nonagrioides (Lef.).
We isolated and characterized two members of the alpha-crystallin/sHsp family, SnoHsp19.5 and SnoHsp20.8 from Sesamia nonagrioides (Lepidoptera: Noctuidae). The cDNAs encoded proteins of 174 and 185 amino acids, with calculated molecular weights of 19.5 and 20.8 kDa, respectively. The deduced amino acid sequences of SnoHsp19.5 and SnoHsp20.8 showed highest homology to Hsp19.7 of Mamestra brassicae and to Bombyx mori Hsp20.4, respectively. Expression patterns of SnoHsp19.5 and SnoHsp20.8 in non-diapausing individuals under different environmental conditions (heat or cold) showed different accumulation profiles for the two genes after heat and cold treatment. SnoHsp19.5 was consistently expressed, while SnoHsp20.8 gene was down-regulated in deep diapause and was up-regulated at the termination of diapause. Our results suggest that these two genes play distinctive roles in the regulation of diapause.
Gkouvitsas
Theodoros
T
Department of Agricultural Biotechnology, Agricultural University of Athens, Iera Odos 75, Athens 11855, Greece.
Kontogiannatos
Dimitris
D
Kourti
Anna
A
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003080:Cold Temperature; D018076:DNA, Complementary / Q000235:genetics; D005786:Gene Expression Regulation / Q000502:physiology*; D006360:Heat-Shock Proteins / Q000235:genetics / Q000378:metabolism*; D006358:Hot Temperature; D008969:Molecular Sequence Data; D009036:Moths / Q000378:metabolism*; D010802:Phylogeny; D013312:Stress, Physiological
D018076:DNA, Complementary; D006360:Heat-Shock Proteins