TY  - JOUR
T1  - Cloning, Sequencing and Expression of a Heat Shock Protein 70 Gene from <i>Tenebrio molitor</i>
AU - Huang, Qiong AU - Wang, Qin AU - Sun, Lin AU - Hu, Jie 
JO  - Journal of Animal and Veterinary Advances
VL  - 11
IS  - 24
SP  - 4632
EP  - 4643
PY  - 2012
DA  - 2001/08/19
SN  - 1680-5593
DO  - javaa.2012.4632.4643
UR  - https://makhillpublications.co/view-article.php?doi=javaa.2012.4632.4643
KW  - stress proteins
KW  -HSPs
KW  -PCR
KW  -shock protein
KW  -HSE
KW  -China
AB  - Heat Shock/Stress Proteins (HSPs) are a group of stress proteins 
  which are closely associated with organisms&#146; adaptability to environment 
  and the heat shock protein 70 is the most conserved and important member. Researchers 
  cloned an <I>hsp70</I> gene from <I>Tenebrio molitor</I> larvae by PCR and RACE 
  Method and determined the mRNA abundance in the beetle developmental stages 
  by real-time qPCR. The cDNA cloned was 2,282 bp in full length containing a 
  115 bp 5'untranslated region rich in adenine, a 1,935 bp open reading frame 
  and a 232 bp 3'untranslated regionrich in adenine and thymine. It also had seven 
  repeats of the Heat Shock Element (HSE) nGAAn in its 5'UTR and a 22 bp Poly 
  (A) tail in the 3'UTR. The deduced heat shock protein had a highly conserved 
  N-terminal ATPase domain and a conserved C-terminal peptide-binding domain. 
  The tertiary structure of ATPase domain was made of two large globular subdomains 
  which were separated by a deep cleft and the peptide-binding domain was a sandwich 
  of 2 four-stranded &#946;-sheets with four loops protruding upwards and two 
  &#945;-helices. Real-time qPCR analysis revealed that the hsp70 mRNA expression 
  in <I>T. molitor</I> was characterized by heat-inducible and developmental-regulation 
  features. The results form a basis for further research on structure, function 
  and expression regulation of HSPs from <I>T. molitor</I> as well as to decipher 
  the relationship between HSPs and stress-resistance in the beetle.
ER  -