Journal
MOLECULAR BIOTECHNOLOGY
Volume 54, Issue 2, Pages 643-650Publisher
HUMANA PRESS INC
DOI: 10.1007/s12033-012-9606-8
Keywords
Dehydrins; beta-Glucosidase; Lactate dehydrogenase; K-segment; Abiotic stress
Funding
- Ministry of Higher Education and Scientific Research, Tunisia
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The wheat dehydrin DHN-5 has been previously shown to exhibit heat protecting effect on enzymatic activities. In order to understand the molecular mechanism by which DHN-5 exerts its protective function, we performed an approach to dissect the functional domains of DHN-5 responsible for this feature. In two distinct enzymatic assays, we found that the truncated forms of DHN-5 containing only one K- or two K-segments are able to protect albeit to less extent than the wild type protein, lactate dehydrogenase and beta-glucosidase against damage induced by various stresses in vitro. However, the YS- and I broken vertical bar-segments alone have no protective effects on these enzymes. Therefore, our study provides the evidence that the protective function of DHN-5 seems to be directly linked to its K-segments which through their amphipatic alpha-helical structure, may act to prevent protein aggregation.
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