Abstract
Studies on the functional roles of dehydrins (DHNs) in heat tolerance of plants are scarce. This study was conducted to immunohistolocalize DHNs in leaves of heat-tolerant (CP-4333) and heat-sensitive (HSF-240) sugarcane (Saccharum officinarum L.) clones at three phenological stages in order to elucidate their putative roles under heat stress. CP-4333 indicated greater amounts of heat-stable proteins than HSF-240 under heat stress. Western blotting revealed the expression of three DHNs in CP-4333 (13- and 15-kDa peptides at 48 h and an additional 18-kDa band at 72 h) and two (13 and 15 kDa at 48 h) in HSF-240 at formative stage; two DHNs in CP-4333 (20 and 25 kDa) and one in HSF-240 (20 kDa) at grand growth stage, while two DHNs in CP-4333 (20 and 22 kDa) and one in HSF-240 (20 kDa) at maturity stage. Tissue-specific immunohistolocalization showed that DHNs were expressed in stele particularly the phloem and the cells intervening bundle sheath and vascular bundles. Furthermore, DHNs were also found scattered along the epidermal and parenchymatous cells. Recovery of sugarcane from heat stress manifested a gradual disappearance of DHNs in both the clones, being quicker in sensitive clone (HSF-240). Results suggested specific implications for DHNs synthesis. Their synthesis in epidermis appears to protect the mesophyll tissues from heat injury. When associated to vascular tissue, they tend to ensure the normal photoassimilate loading into the sieve element–companion cell complex. DHNs diminution during recovery suggested that their expression was transitory. However, prolonged retention of DHNs by tolerant clone appears to be an adaptive advantage of sugarcane to withstand heat stress.
Similar content being viewed by others
References
Bravo LA, Close TJ, Corcuera LJ, Guy CL (1999) Characterization of an 80-kDa dehydrin-like protein in barley responsive to cold acclimation. Physiol Plant 106:177–183
Bravo LA, Gallardo J, Navarrete A, Olave N, MartInez J, Alberdi M, Close TJ, Corcuera LJ (2003) Cryoprotective activity of a cold-induced dehydrin purified from barley. Physiol Plant 118:262–269
Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248–254
Cuming AC (1999) LEA proteins. In: Casey R, Shewry PR (eds) Seed proteins. Kluwer, Dordrecht, pp 753–780
Close TJ (1996) Dehydrins: emergence of a biochemical role of a family of plant dehydration proteins. Physiol Plant 97:795–803
Close TJ (1997) Dehydrins: a commonality in the response of plants to dehydration and low temperature. Physiol Plant 100:291–296
Close TJ, Fenton RD, Moonan F (1993) A view of plant dehydrins using antibodies specific to the carboxy terminal peptide. Plant Mol Biol 23:279–286
Godoy JA, Lunar R, Torresschumann S, Moreno J, Rodrigo RM, Pintortoro JA (1994) Expression, tissue distribution and subcellular-localization of dehydrin TAS14 in salt stressed tomato plants. Plant Mol Biol 26:1921–1934
Goyal K, Walton LJ, Tunnacliffe A (2005) LEA proteins prevent protein aggregation due to water stress. Biochem J 388:151–157
Halford NG (2009) New insights on the effects of heat stress on crops. J Exp Bot 60:4215–4216
Hanin M, Brini F, Ebel C, Toda Y, Takeda S, Masmoudi K (2011) Plant dehydrins and stress tolerance versatile proteins for complex mechanisms. Plant Signal Behav 6:1–7
Heyen BJ, Alsheikh MK, Smith EA, Torvik CF, Seals DF, Randall SK (2002) The calcium-binding activity of a vacuole-associated, dehydrin like protein is regulated by phosphorylation. Plant Physiol 130:675–687
Houde M, Daniel C, Lachapelle M, Allard F, Laliberte S, Sarhan F (1995) Immunolocalization of freezing-tolerance-associated proteins in the cytoplasm and nucleoplasm of wheat crown tissues. Plant J 8:583–593
Hara M, Terashima S, Kuboi T (2001) Characterization and cryoprotective activity of cold-responsive dehydrin from Citrus unshiu. J Plant Physiol 58:1333–1339
Karlson DT, Fujino T, Kimura S, Baba K, Itoh T, Ashworth EN (2003) Novel plasmodesmata association of dehydrin-like proteins in cold acclimation red-osier dogwood (Cornus sericea). Tree Physiol 23:759–767
Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of the bacteriophage T4. Nature 227:680–685
Mahmood S, Wahid A, Javed A, Basra SMA (2010) Heat stress effects on forage quality characteristics of maize (Zea mays) cultivars. Int J Agric Biol 12:701–706
Nylander M, Svensson J, Palva ET, Welin BV (2001) Stress-induced accumulation and tissue-specific localisation of dehydrins in Arabidopsis thaliana. Plant Mol Biol 45:263–279
Reyes D, Rodríguez D, Lorenzo O, Nicolás G, Cañas R, Cantón FR, Canovas FM, Nicolás C (2006) Immunolocalization of FsPK1 correlates this abscisic acid-induced protein kinase with germination arrest in Fagus sylvatica L. seeds. J Exp Bot 57:923–929
Rinne PLH, Kaikuranta PLM, van der Plas LHW, van der Schoot C (1999) Dehydrins in cold-acclimated apices of birch (Betula pubescens Ehrh.): production, localization and potential role in rescuing enzyme function during dehydration. Planta 209:377–388
Rorat T, Szabala BM, Grygorowicz WJ, Wojtowicz B, Yin Z, Rey P (2006) Expression of SK3-type dehydrin in transporting organs is associated with cold acclimation in Solanum species. Planta 224:205–221
Rurek M (2010) Diverse accumulation of several dehydrin-like proteins in cauliflower (Brassica oleracea var. botrytis), Arabidopsis thaliana and yellow lupin (Lupinus luteus) mitochondria under cold and heat stress. BMC Plant Biol 10:181
Ruzin SE (1999) Plant microtechnique and microscopy. Oxford University Press, New York
Schoffl F, Prandl R, Reindl A (1999) Molecular responses to heat stress. In: Shinozaki K, Yamaguchi-Shinozaki K (eds) Molecular responses to cold, drought, heat and salt stress in higher plants. K.R.G. Landes Co., Austin, pp 81–98
Taiz L, Zeiger E (2010) Plant physiology, 5th edn. Sinauer Associates Inc. Publishers, Sunderland
Tompa P (2005) The interplay between structure and function in intrinsically unstructured proteins. FEBS Lett 579:3346–3354
Towbin H, Staehlin T, Gordon J (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci U S A 76:4350–4354
Wisniewski M, Webb R, Balsamo R, Close TJ, Yu XM, Griffith M (1999) Purification, immunolocalization, cryoprotective, and antifreeze activity of PCA60: a dehydrin from peach (Prunus persica). Physiol Plant 105:600–608
Wahid A, Close TJ (2007) Expression of dehydrins under heat stress and their relationship with water relations of sugarcane leaves. Biol Plant 51:104–109
Wahid A, Gelani S, Ashraf M, Foolad MR (2007) Heat tolerance in plants: an overview. Environ Exp Bot 61:199–223
Wolkers WF, McCready S, Brandt WF, Lindsey GG, Hoekstra FA (2001) Isolation and characterization of a D-7 LEA protein from pollen that stabilizes glasses in vitro. Biochim Biophys Acta 1544:196–206
You W (2012) Research on isolation of 69.5kD heat-stable protein in Zea mays seedling roots under different stress and its expression regulation. Available at: http://www.agrpaper.com/tag/heat-stable-protein. Accessed 11 June 2012
Acknowledgments
This study was financially supported by the Higher Education Commission of Pakistan. We highly appreciate the microtomy facility provided by Prof. Zargham and Prof. Ahrar, Univ. Agric., Faisalabad, Pakistan and the DHNs antibodies gift from Prof. Tim Close, UCR, USA. This paper is part of the PhD. thesis of the first author.
Conflict of interest
There is no conflict of interest regarding this paper.
Author information
Authors and Affiliations
Corresponding author
Additional information
Handling Editor: Bhumi Nath Tripathi
Rights and permissions
About this article
Cite this article
Galani, S., Wahid, A. & Arshad, M. Tissue-specific expression and functional role of dehydrins in heat tolerance of sugarcane (Saccharum officinarum). Protoplasma 250, 577–583 (2013). https://doi.org/10.1007/s00709-012-0443-1
Received:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1007/s00709-012-0443-1