Jump to Main Content
Identification and functional characterization of Siberian wild rye (Elymus sibiricus L.) small heat shock protein 16.9 gene (EsHsp16.9) conferring diverse stress tolerance in prokaryotic cells
- Lee, Sang-Hoon, Lee, Ki-Won, Lee, Dong-Gi, Son, Daeyoung, Park, Su Jung, Kim, Ki-Yong, Park, Hyung Soo, Cha, Joon-Yung
- Biotechnology letters 2015 v.37 no.4 pp. 881-890
- Elymus sibiricus, Northern blotting, cell growth, denaturation, drought, gene expression, genes, heat, heat shock proteins, malate dehydrogenase, messenger RNA, open reading frames, paraquat, polyethylene glycol, prokaryotic cells, rye, sodium chloride, stress tolerance
- Small heat shock proteins (Hsps) protect against stress-inducible denaturation of substrates. Our objectives were to clone and examine the mRNA expression of the Hsp16.9 gene from Siberian wild rye grown under diverse stress treatments. We characterized EsHsp16.9 from Elymus sibiricus L. EsHsp16.9 has a 456-bp open reading frame that encodes a 151-amino acid protein with a conserved α-crystallin domain. Northern blot analysis showed that EsHsp16.9 transcripts were enhanced by heat, drought, arsenate, methyl viologen, and H₂O₂treatment. In addition, recombinant EsHsp16.9 protein acts as a molecular chaperone to prevent the denaturation of malate dehydrogenase. Growth of cells overexpressing EsHsp16.9 was up to 200 % more rapid in the presence of NaCl, arsenate, and polyethylene glycol than that of cells harboring an empty vector. These data suggest that EsHsp16.9 acts as a molecular chaperone that enhances stress tolerance in living organisms.