Identification and expression analyses of two lotus (Nelumbo nucifera) dehydrin genes in response to adverse temperatures, ABA and IAA treatments

Chen Dong; Meigui Yang; Huanhuan Wang; Junpeng Mi

doi:10.1515/biolog-2017-0080

Article

Identification and expression analyses of two lotus (Nelumbo nucifera) dehydrin genes in response to adverse temperatures, ABA and IAA treatments

Chen Dong , Meigui Yang , Huanhuan Wang and Junpeng Mi

Published/Copyright: July 31, 2017

Published by

Become an author with De Gruyter Brill

Author Information Explore this Subject

From the journal Biologia Volume 72 Issue 7

Abstract

Dehydrins (DHNs) play imperative role in the stress tolerance of high plants. In this study, the YSK₂-type DHN (NnDHNl) and SK₃-type DHN (NnDHN2) were investigated. The putative NnDHNl and NnDNH2 shared conserved S-segment as well as K-segment, with distinct isoelectric points, kinase selectivities and number of functional motifs. Phylogenetic analysis revealed that NnDHNs were grouped with Y_nSK_n- and SK_n-type of DHNs in high plants. Additionally,NnDHN1 mRNA was only expressed in leaves and embryo. NnDHN2 mRNA was found in embryo, leaves, rhizome and leafstalk.NnDHNs mRNAs were not detected in root of N. nucifera. Real-time PCR assay demonstrated that the levels of NnDHN1 and NnDHN2 mRNAs were significantly elevated during cold temperature, while both were relatively stable in response to high temperature. Moreover, NnDHN2 mRNA was significantly increased after treatment with abscisic acid (ABA) or indole-3-acetic acid (IAA), while NnDHN1 mRNA was induced by ABA treatment with little change in response to IAA. These results illustrate two NnDHNs with partially overlapping function which exhibit different stress responsiveness.

Key words: Nelumbo nucifera; dehydrins; organ specific expression; plant hormone treatment

Acknowledgements

The authors are greatly appreciative of the reviewers for their helpful comments and detailed suggestions. This work is financially supported by National Natural Science Foundation of China (no. 31601366), Foundation of Henan Educational Committee (no. 16A180024), Doctoral Scientific Research Start-up Foundation from Henan University of Technology (no. 31400855) and Fundamental Research Funds for the Henan Provincial Colleges and Universities in Henan University of Technology (no. 2015QNJH07).

References

Alsheikh M.K., Svensson J. & Randall S.K. 2005. Phosphorylation regulated ion-binding is a property shared by the acidic subclass dehydrins. Plant Cell Environ. 28:1114–1122.10.1111/j.1365-3040.2005.01348.xSearch in Google Scholar

Babic M., Radic S., Cvjetko P., Roje V., Pevalek-Kozlina B. & Pavlica M. 2009. Antioxidative response of Lemna minor plants exposed to thallium (I)-acetate. Aquatic Bot. 91:166–172.10.1016/j.aquabot.2009.05.005Search in Google Scholar

Bies-Etheve N., Gaubier-Comella P., Debures A., Lasserre E., Jobet E., Raynal M., Cooke R. & Delseny M. 2008. Inventory, evolution and expression profiling diversity of the LEA (late embryogenesis abundant) protein gene family in Arabidopsis thaliana. Plant. Mol. Biol.67:107–124.10.1007/s11103-008-9304-xSearch in Google Scholar PubMed

Brini F., Yamamoto A., Jlaiel L., Takeda S., Hobo T., Dinh H.Q., Hattori T., Masmoudi K. & Hanin M. 2011. Pleiotropic effects of the wheat dehydrin DHN-5 on stress responses in Arabidopsis. Plant Cell Physiol.52: 676–688.10.1093/pcp/pcr030Search in Google Scholar PubMed

Dong C., Zheng X., Diao Y., Wang Y., Zhou M. & Hu Z. 2015. Molecular cloning and expression analysis of a catalase gene (NnCAT) from Nelumbo nucifera. Appl. Biochem. Biotechnol. 177: 1216–1228.10.1007/s12010-015-1808-7Search in Google Scholar PubMed

Eriksson S.K., Kutzer M., Procek J., Grobner G. & Harryson P. 2011. Tunable membrane binding of the intrinsically disordered dehydrin Lti30, a cold-induced plant stress protein. Plant Cell 23: 2391–2404.10.1105/tpc.111.085183Search in Google Scholar PubMed PubMed Central

Hara M., Shinoda Y., Tanaka Y. & Kuboi T. 2009. DNA binding of citrus dehydrin promoted by zinc ion. Plant Cell Environ. 32: 532–541.10.1111/j.1365-3040.2009.01947.xSearch in Google Scholar PubMed

Hughes S. & Graether S.P. 2011. Cryoprotective mechanism of a small intrinsically disordered dehydrin protein. Protein Sci. 20: 42–50.10.1002/pro.534Search in Google Scholar PubMed PubMed Central

Hundertmark M. & Hincha D.K. 2008. LEA (Late Embryogenesis Abundant) proteins and their encoding genes in Arabidopsis thaliana. BMC Genomics 9:118.10.1186/1471-2164-9-118Search in Google Scholar PubMed PubMed Central

Hundertmark M., Buitink J., Leprince O. & Hincha D.K. 2011. Reduction of seed-specific dehydrins reduces seed longevity in Arabidopsis thaliana. Seed Sci. Res. 21:165–173.10.1017/S0960258511000079Search in Google Scholar

Kim S.Y. & Nam K.H. 2010. Physiological roles of ERD10 in abiotic stresses and seed germination of Arabidopsis. Plant Cell Rep. 29: 203–209.10.1007/s00299-009-0813-0Search in Google Scholar PubMed

Koag M.C., Wilkens S., Fenton R.D., Resnik J., Vo E. & Close TJ. 2009. The K-segment of maize DHN1 mediates binding to anionic phospholipid vesicles and concomitant structural changes. Plant. Physiol. 150: 1503–1514.10.1104/pp.109.136697Search in Google Scholar PubMed PubMed Central

Lescot M., Dehais P., Thijs G., Marchal K., Moreau Y., Van de peer Y., Rouze P. & Rombauts S. 2002. PlantCARE, a database of plant cis-acting regulatory elements and a portal to tools for in silico analysis of promoter sequences. Nucleic Acids Res. 30: 325–327.10.1093/nar/30.1.325Search in Google Scholar PubMed PubMed Central

Livak K.J. & Schmittgen T.D. 2001. Analysis of relative gene expression data using real-time quantitative PCR and the 2^−ΔΔ CT method. Methods (San Diego, Calif.). 25: 402–408.10.1006/meth.2001.1262Search in Google Scholar PubMed

Peng Y., Reyes J.L., Wei H., Yang Y., Karlson D., Covarrubias A.A., Krebs S.L., Fessehaie A. & Arora R. 2008. RcDhn5, a cold acclimation-responsive dehydrin from Rhododendron catawbiense rescues enzyme activity from dehydration effects in vitro and enhances freezing tolerance in RcDhn5-overexpressing Arabidopsis plants. Physiol. Plant. 134: 583–597.10.1111/j.1399-3054.2008.01164.xSearch in Google Scholar PubMed

Priestley D.A. & Posthumus M.A. 1982. Extreme longevity of lotus seeds from Pulantien. Nature 299: 148–149.10.1038/299148a0Search in Google Scholar

Riera M., Figueras M., Lopez C., Goday A. & Pages M. 2004. Protein kinase CK2 modulates developmental functions of the abscisic acid responsive protein Rab17 from maize. Proc. Natl. Acad. Sci. USA 101:9879–9884.10.1073/pnas.0306154101Search in Google Scholar PubMed PubMed Central

Shekhawat U.K., Srinivas L & Ganapathi T.R. 2011. MusaDHN1, a novel multiple stress-inducible SK3-type dehydrin gene, contributes affirmatively to drought- and salt-stress tolerance in banana. Planta 234: 915.10.1007/s00425-011-1455-3Search in Google Scholar PubMed

Shen-Miller J., Lindner P., Xie Y., Villa S., Wooding K., Clarke S.G., Loo R.R. & Loo J.A. 2013. Thermal-stable proteins of fruit of long-living sacred Lotus Nelumbo nucifera Gaertn var. China Antique. Tropical. Plant. Biol.6: 69–84.10.1007/s12042-013-9124-2Search in Google Scholar PubMed PubMed Central

Sridhar K.R. & Bhat R. 2007. Lotus-A potential nutraceutical source. J. Agric. Technol. 3: 143–145.Search in Google Scholar

Tamura K., Dudley J., Nei M. & Kumar S. 2007. MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0. Mol. Biol. Evol. 24: 1596–1599.10.1093/molbev/msm092Search in Google Scholar PubMed

Vaseva I.I., Anders I., Yuperlieva-Mateeva B., Nenkova R., Kostadinova A. & Feller U. 2014a. Dehydrin expression as a potential diagnostic tool for cold stress in white clover. Plant. Physiol. Biochem. 78: 43–48.10.1016/j.plaphy.2014.02.014Search in Google Scholar PubMed

Vaseva I.I., Anders I. & Feller U. 2014b. Identification and expression of different dehydrin subclasses involved in drought response of Trifolium repens. J. Plant. Physiol. 171: 213–224.10.1016/j.jplph.2013.07.013Search in Google Scholar PubMed

Wang X., Zhu H., Jin G., Liu H., Wu W. & Zhu J. 2007. Genomescale identification and analysis of LEA genes in rice (Oryza sativa L.). Plant. Sci. 172: 414–420.10.1016/j.plantsci.2006.10.004Search in Google Scholar

Xu J., Zhang Y., Guan Z., Wei W., Han L. & Chai T. 2008. Expression and function of two dehydrins under environmental stresses in Brassica juncea L. Mol. Breeding 21: 431–438.10.1007/s11032-007-9143-5Search in Google Scholar

Xu Y. & Crouch J. 2008. Marker-assisted selection in plant breeding: from publi-cations to practice. Crop Sci. 48: 391–407.10.2135/cropsci2007.04.0191Search in Google Scholar

Yamasaki Y., Koehler G., Blacklock B.J. & Randall S.K. 2013. Dehydrin expression in soybean. Plant Physiol. Biochem. 70: 213–220.10.1016/j.plaphy.2013.05.013Search in Google Scholar PubMed

Yang Y., He M., Zhu Z., Li S., Xu Y., Zhang C., Singer S.D. & Wang Y. 2012. Identification of the dehydrin gene family from grapevine species and analysis of their responsiveness to various forms of abiotic and biotic stress. BMC Plant Biol. 12: 140.10.1186/1471-2229-12-140Search in Google Scholar PubMed PubMed Central

Received: 2016-11-20

Accepted: 2017-2-27

Published Online: 2017-7-31

Published in Print: 2017-7-26

You are currently not able to access this content.

Articles in the same Issue

https://doi.org/10.1515/biolog-2017-0080

Keywords for this article

Nelumbo nucifera; dehydrins; organ specific expression; plant hormone treatment