Abstract
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 β-glucosidase against damage induced by various stresses in vitro. However, the YS- and Φ-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 α-helical structure, may act to prevent protein aggregation.
Original language | English |
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Pages (from-to) | 643-650 |
Number of pages | 8 |
Journal | Molecular Biotechnology |
Volume | 54 |
Issue number | 2 |
DOIs | |
Publication status | Published - Jun 2013 |
Externally published | Yes |
Keywords
- Abiotic stress
- Dehydrins
- K-segment
- Lactate dehydrogenase
- β-Glucosidase
ASJC Scopus subject areas
- Biotechnology
- Bioengineering
- Biochemistry
- Applied Microbiology and Biotechnology
- Molecular Biology