Abstract
Dehydrin improves plant resistance to many abiotic stresses. In this study, the expression profiles of a dehydrin gene, CdDHN4, were estimated under various stresses and abscisic acid (ABA) treatments in two bermudagrasses (Cynodon dactylon L.): Tifway (drought-tolerant) and C299 (drought-sensitive). The expression of CdDHN4 was up-regulated by high temperatures, low temperatures, drought, salt and ABA. The sensitivity of CdDHN4 to ABA and the expression of CdDHN4 under drought conditions were higher in Tifway than in C299. A 1239-bp fragment, CdDHN4-P, the partial upstream sequence of the CdDHN4 gene, was cloned by genomic walking from Tifway. Bioinformatic analysis showed that the CdDHN4-P sequence possessed features typical of a plant promoter and contained many typical cis elements, including a transcription initiation site, a TATA-box, an ABRE, an MBS, a MYC, an LTRE, a TATC-box and a GT1-motif. Transient expression in tobacco leaves demonstrated that the promoter CdDHN4-P can be activated by ABA, drought and cold. These results indicate that CdDHN4 is regulated by an ABA-dependent signal pathway and that the high sensitivity of CdDHN4 to ABA might be an important mechanism enhancing the drought tolerance of bermudagrass.
Highlights
Dehydrins accumulate in embryogenesis during seed maturation and in vegetative tissue in response to drought, salinity or cold (Dure et al, 1981; Close, 1996; Hara et al, 2013)
The promoter of the abscisic acid (ABA)-inducible gene dhn1 in barely contains a TACGTCC fragment consisting of a G-box and GC-motif, and its removal was accompanied by loss of promoter sensitivity to ABA (Robertson et al, 1995)
Amar found the cis-regulatory elements ABA-responsive elements (ABREs) in wheat PrDHN-5; these elements are required for abiotic stress and ABA responsiveness (Amar et al, 2013)
Summary
Dehydrins (group-II late embryogenesis abundant proteins) accumulate in embryogenesis during seed maturation and in vegetative tissue in response to drought, salinity or cold (Dure et al, 1981; Close, 1996; Hara et al, 2013). These proteins are hydrophilic proteins that contain three conserved motifs: the K, Y, and S segments (Rorat, 2006; Eriksson et al, 2011; Hara et al, 2011).
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