A dehydrin-dehydrin interaction: the case of SK3 from Opuntia streptacantha
| Autor: | Juan Francisco Jiménez-Bremont, Itzell E. Hernández-Sánchez, Aída Araceli Rodríguez-Hernández, David M. Martynowicz, Maria B. Pérez-Morales, Steffen P. Graether |
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| Jazyk: | angličtina |
| Rok vydání: | 2014 |
| Předmět: |
0106 biological sciences
Circular dichroism yeast two-hybrid In silico Two-hybrid screening Transgene homodimer Size-exclusion chromatography Plant Science Biology lcsh:Plant culture Intrinsically disordered proteins 01 natural sciences 03 medical and health sciences Arabidopsis lcsh:SB1-1110 Original Research Article K-segments 030304 developmental biology Genetics 0303 health sciences histidine-rich region biology.organism_classification Yeast intrinsically disordered proteins Cell biology SK3-dehydrin 010606 plant biology & botany |
| Zdroj: | Frontiers in Plant Science, Vol 5 (2014) Frontiers in Plant Science |
| ISSN: | 1664-462X |
| DOI: | 10.3389/fpls.2014.00520 |
| Popis: | Dehydrins belongs to a large group of highly hydrophilic proteins known as Late Embryogenesis Abundant (LEA) proteins. It is well known that dehydrins are intrinsically disordered plant proteins that accumulate during the late stages of embryogenesis and in response to abiotic stresses; however, the molecular mechanisms by which their functions are carried out are still unclear. We have previously reported that transgenic Arabidopsis plants overexpressing an Opuntia streptacantha SK3 dehydrin (OpsDHN1) show enhanced tolerance to freezing stress. Herein, we show using a split-ubiquitin yeast two-hybrid system that OpsDHN1 dimerizes. We found that the deletion of regions containing K-segments and the histidine-rich region in the OpsDHN1 protein affects dimer formation. Not surprisingly, in silico protein sequence analysis suggests that OpsDHN1 is an intrinsically disordered protein, an observation that was confirmed by circular dichroism and gel filtration of the recombinantly expressed protein. The addition of zinc triggered the association of recombinantly expressed OpsDHN1 protein, likely through its histidine-rich motif. These data brings new insights about the molecular mechanism of the OpsDHN1 SK3-dehydrin. |
| Databáze: | OpenAIRE |
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