Plant Heat Shock Protein Families: Essential Machinery for Development and Defense

  • Anshulika Sable Plant Molecular Biology Laboratory, National Botanical Research Institute, Rana Pratap Marg, Lucknow 226001, India
  • Sudhir K Agarwal Department of Biochemistry, University of Lucknow, Lucknow 226007, India


Being sessile in nature, plants experience stress due to constantly changing environmental conditions such as drought, salt stress, exposure to chemicals along with highly variable temperature (heat and cold) stress in the era of global warming. Heat shock proteins (HSPs) are a group of proteins, which help plants to cope the adverse conditions caused by these stresses. HSPs help to maintain the cellular homeostasis by maintaining the three-dimensional structure of cellular proteins. Apart from homeostasis maintenance during various stress conditions, these molecular chaperons are also involved in maintaining the normal cellular processes such as protein folding/unfolding, multi-protein complex assembly, protein sorting and transport to correct locations. Presence of high to low molecular weight HSP classes in plant genome points towards a precisely evolved adaptation mechanism. These classes include HSP100, HSP90, HSP70, HSP60, and sHSPs. Here, we have discussed the various classes of HSP proteins with emphasis on their mechanism of action, their evolution across the plant kingdom along with their role in combating the stress.


Agarwal, M., Katiyar-Agarwal, S., Sahi, C., Gallie, D.R., and Grover, A. (2001). Arabidopsis thaliana Hsp100 proteins: kith and kin. Cell stress & chaperones 6:219-224.
Ali, M.M., Roe, S.M., Vaughan, C.K., Meyer, P., Panaretou, B., Piper, P.W., Prodromou, C., and Pearl, L.H. (2006). Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex. Nature 440:1013.
Bardwell, J., and Craig, E.A. (1984). Major heat shock gene of Drosophila and the Escherichia coli heat-inducible dnaK gene are homologous. Proceedings of the National Academy of Sciences 81:848-852.
Bekh-Ochir, D., Shimada, S., Yamagami, A., Kanda, S., Ogawa, K., Nakazawa, M., Matsui, M., Sakuta, M., Osada, H., and Asami, T. (2013). A novel mitochondrial DnaJ/Hsp40 family protein BIL2 promotes plant growth and resistance against environmental stress in brassinosteroid signaling. Planta 237:1509-1525.
Berruti, G., Perego, L., Borgonovo, B., and Martegani, E. (1998). MSJ-1, a new member of the DNAJ family of proteins, is a male germ cell-specific gene product. Experimental cell research 239:430-441.
Borges, J.C., and Ramos, C.H. (2009). Characterization of nucleotide-induced changes on the quaternary structure of human 70 kDa heat shock protein Hsp70. 1 by analytical ultracentrifugation. BMB reports.
Bork, P., Sander, C., Valencia, A., and Bukau, B. (1992). A module of the DnaJ heat shock proteins found in malaria parasites. Trends in biochemical sciences 17:129.
Bösl, B., Grimminger, V., and Walter, S. (2006). The molecular chaperone Hsp104—a molecular machine for protein disaggregation. Journal of structural biology 156:139-148.
Burton, B.M., and Baker, T.A. (2005). Remodeling protein complexes: insights from the AAA+ unfoldase ClpX and Mu transposase. Protein science 14:1945-1954.
Büyük, İ., Inal, B., Ilhan, E., Tanriseven, M., Aras, S., and Erayman, M. (2016). Genome-wide identification of salinity responsive HSP70s in common bean. Molecular biology reports 43:1251-1266.
Cao, D., Froehlich, J.E., Zhang, H., and Cheng, C.L. (2003). The chlorate‐resistant and photomorphogenesis‐defective mutant cr88 encodes a chloroplast‐targeted HSP90. The Plant Journal 33:107-118.
Cashikar, A.G., Duennwald, M., and Lindquist, S.L. (2005). A chaperone pathway in protein disaggregation Hsp26 alters the nature of protein aggregates to facilitate reactivation by Hsp104. Journal of Biological Chemistry 280:23869-23875.
Cheetham, M.E., Brion, J.-P., and Anderton, B.H. (1992). Human homologues of the bacterial heat-shock protein DnaJ are preferentially expressed in neurons. Biochemical Journal 284:469-476.
Chen, K.-M., Holmström, M., Raksajit, W., Suorsa, M., Piippo, M., and Aro, E.-M. (2010). Small chloroplast-targeted DnaJ proteins are involved in optimization of photosynthetic reactions in Arabidopsis thaliana. BMC plant biology 10:43.
Chen, K.-M., Piippo, M., Holmström, M., Nurmi, M., Pakula, E., Suorsa, M., and Aro, E.-M. (2011). A chloroplast-targeted DnaJ protein AtJ8 is negatively regulated by light and has rapid turnover in darkness. Journal of plant physiology 168:1780-1783.
DeRocher, A., and Vierling, E. (1995). Cytoplasmic HSP70 homologues of pea: differential expression in vegetative and embryonic organs. Plant molecular biology 27:441-456.
Dragovic, Z., Broadley, S.A., Shomura, Y., Bracher, A., and Hartl, F.U. (2006). Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s. The EMBO journal 25:2519-2528.
Duck, N., McCormick, S., and Winter, J. (1989). Heat shock protein hsp70 cognate gene expression in vegetative and reproductive organs of Lycopersicon esculentum. Proceedings of the National Academy of Sciences 86:3674-3678.
Duck, N.B., and Folk, W.R. (1994). Hsp70 heat shock protein cognate is expressed and stored in developing tomato pollen. Plant molecular biology 26:1031-1039.
Eyles, S.J., and Gierasch, L.M. (2010). Nature’s molecular sponges: small heat shock proteins grow into their chaperone roles. Proceedings of the National Academy of Sciences 107:2727-2728.
Fan, F., Yang, X., Cheng, Y., Kang, Y., and Chai, X. (2017). The DnaJ Gene Family in Pepper (Capsicum annuum L.): Comprehensive Identification, Characterization and Expression Profiles. Frontiers in plant science 8:689.
Fietto, L.G., Costa, M.D., Cruz, C.D., Souza, A.A., Machado, M.A., and Fontes, E.P. (2007). Identification and in silico analysis of the Citrus HSP70 molecular chaperone gene family. Genetics and Molecular Biology 30:881-887.
Frydman, J. (2001). Folding of newly translated proteins in vivo: the role of molecular chaperones. Annual review of biochemistry 70:603-647.
Gething, M.-J. (1997). Guidebook to molecular chaperones and protein-folding catalysts: OUP Oxford.
Glover, J.R., and Lindquist, S. (1998). Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins. Cell 94:73-82.
Guo, M., Liu, J.-H., Lu, J.-P., Zhai, Y.-F., Wang, H., Gong, Z.-H., Wang, S.-B., and Lu, M.-H. (2015). Genome-wide analysis of the CaHsp20 gene family in pepper: comprehensive sequence and expression profile analysis under heat stress. Frontiers in plant science 6:806.
Guo, M., Liu, J.-H., Ma, X., Zhai, Y.-F., Gong, Z.-H., and Lu, M.-H. (2016). Genome-wide analysis of the Hsp70 family genes in pepper (Capsicum annuum L.) and functional identification of CaHsp70-2 involvement in heat stress. Plant Science 252:246-256.
Guy, C.L., and Li, Q.-B. (1998). The organization and evolution of the spinach stress 70 molecular chaperone gene family. The Plant Cell 10:539-556.
Hänninen, A.-L., Simola, M., Saris, N., and Makarow, M. (1999). The cytoplasmic chaperone hsp104 is required for conformational repair of heat-denatured proteins in the yeast endoplasmic reticulum. Molecular biology of the cell 10:3623-3632.
Harrison, B., and Masson, P.H. (2008). Do ARG1 and ARL2 form an actin-based gravity-signaling chaperone complex in root statocytes? Plant signaling & behavior 3:650-653.
Hartl, F.U., Bracher, A., and Hayer-Hartl, M. (2011). Molecular chaperones in protein folding and proteostasis. Nature 475:324.
Hendrick, J.P., and Hartl, F.-U. (1993). Molecular chaperone functions of heat-shock proteins. Annual review of biochemistry 62:349-384.
Hilton, G.R., Lioe, H., Stengel, F., Baldwin, A.J., and Benesch, J.L. (2012). Small heat-shock proteins: paramedics of the cell. In: Molecular Chaperones: Springer. 69-98.
Hong, S.W., and Vierling, E. (2001). Hsp101 is necessary for heat tolerance but dispensable for development and germination in the absence of stress. The Plant Journal 27:25-35.
Hubert, D.A., Tornero, P., Belkhadir, Y., Krishna, P., Takahashi, A., Shirasu, K., and Dangl, J.L. (2003). Cytosolic HSP90 associates with and modulates the Arabidopsis RPM1 disease resistance protein. The EMBO journal 22:5679-5689.
Imai, J., Maruya, M., Yashiroda, H., Yahara, I., and Tanaka, K. (2003). The molecular chaperone Hsp90 plays a role in the assembly and maintenance of the 26S proteasome. The EMBO journal 22:3557-3567.
Ishiguro, S., Watanabe, Y., Ito, N., Nonaka, H., Takeda, N., Sakai, T., Kanaya, H., and Okada, K. (2002). SHEPHERD is the Arabidopsis GRP94 responsible for the formation of functional CLAVATA proteins. The EMBO journal 21:898-908.
Kamada, M., Higashitani, A., and Ishioka, N. (2005). Proteomic analysis of Arabidopsis root gravitropism. Biological Sciences in Space 19:148-154.
Kampinga, H.H., and Craig, E.A. (2010). The HSP70 chaperone machinery: J proteins as drivers of functional specificity. Nature reviews Molecular cell biology 11:579.
Kampinga, H.H., Hageman, J., Vos, M.J., Kubota, H., Tanguay, R.M., Bruford, E.A., Cheetham, M.E., Chen, B., and Hightower, L.E. (2009). Guidelines for the nomenclature of the human heat shock proteins. Cell Stress and Chaperones 14:105-111.
Kim, B.H., and Schöffl, F. (2002). Interaction between Arabidopsis heat shock transcription factor 1 and 70 kDa heat shock proteins. Journal of Experimental Botany 53:371-375.
Kong, F., Deng, Y., Wang, G., Wang, J., Liang, X., and Meng, Q. (2014). LeCDJ1, a chloroplast DnaJ protein, facilitates heat tolerance in transgenic tomatoes. Journal of integrative plant biology 56:63-74.
Kong, F., Deng, Y., Zhou, B., Wang, G., Wang, Y., and Meng, Q. (2013). A chloroplast-targeted DnaJ protein contributes to maintenance of photosystem II under chilling stress. Journal of experimental botany 65:143-158.
Koning, A.J., Rose, R., and Comai, L. (1992). Developmental expression of tomato heat-shock cognate protein 80. Plant physiology 100:801-811.
Krishna, P., and Gloor, G. (2001). The Hsp90 family of proteins in Arabidopsis thaliana. Cell stress & chaperones 6:238-246.
Krishna, P., Sacco, M., Cherutti, J.F., and Hill, S. (1995). Cold-induced accumulation of hsp90 transcripts in Brassica napus. Plant Physiology 107:915-923.
Kumar, R., Singh, A.K., Lavania, D., Siddiqui, M.H., Al-Whaibi, M.H., and Grover, A. (2016). Expression analysis of ClpB/Hsp100 gene in faba bean (Vicia faba L.) plants in response to heat stress. Saudi journal of biological sciences 23:243-247.
Lambert, W., Koeck, P.J., Ahrman, E., Purhonen, P., Cheng, K., Elmlund, D., Hebert, H., and Emanuelsson, C. (2011). Subunit arrangement in the dodecameric chloroplast small heat shock protein Hsp21. Protein Science 20:291-301.
Latijnhouwers, M., Xu, X.-M., and Møller, S.G. (2010). Arabidopsis stromal 70-kDa heat shock proteins are essential for chloroplast development. Planta 232:567-578.
Lee, U., Rioflorido, I., Hong, S.W., Larkindale, J., Waters, E.R., and Vierling, E. (2007). The Arabidopsis ClpB/Hsp100 family of proteins: chaperones for stress and chloroplast development. The Plant Journal 49:115-127.
Li, J., Xiang, C.-Y., Yang, J., Chen, J.-P., and Zhang, H.-M. (2015). Interaction of HSP20 with a viral RdRp changes its sub-cellular localization and distribution pattern in plants. Scientific reports 5.
Li, Q.-B., and Guy, C.L. (2001). Evidence for non-circadian light/dark-regulated expression of Hsp70s in spinach leaves. Plant physiology 125:1633-1642.
Lin, M.-y., Chai, K.-h., Ko, S.-s., Kuang, L.-y., Lur, H.-S., and Charng, Y.-y. (2014). A positive feedback loop between HEAT SHOCK PROTEIN101 and HEAT STRESS-ASSOCIATED 32-KD PROTEIN modulates long-term acquired thermotolerance illustrating diverse heat stress responses in rice varieties. Plant physiology 164:2045-2053.
Lindquist, S., and Craig, E. (1988). The heat-shock proteins. Annual review of genetics 22:631-677.
Liu, Q., and Hendrickson, W.A. (2007). Insights into Hsp70 chaperone activity from a crystal structure of the yeast Hsp110 Sse1. Cell 131:106-120.
Liu, Y., Burch-Smith, T., Schiff, M., Feng, S., and Dinesh-Kumar, S.P. (2004). Molecular chaperone Hsp90 associates with resistance protein N and its signaling proteins SGT1 and Rar1 to modulate an innate immune response in plants. Journal of Biological Chemistry 279:2101-2108.
Lomiwes, D., Farouk, M., Wiklund, E., and Young, O. (2014). Small heat shock proteins and their role in meat tenderness: A review. Meat Science 96:26-40.
Lopes-Caitar, V.S., de Carvalho, M.C., Darben, L.M., Kuwahara, M.K., Nepomuceno, A.L., Dias, W.P., Abdelnoor, R.V., and Marcelino-Guimarães, F.C. (2013). Genome-wide analysis of the Hsp 20 gene family in soybean: comprehensive sequence, genomic organization and expression profile analysis under abiotic and biotic stresses. BMC genomics 14:577.
Lopes-Caitar, V.S., Silva, S.M.H., and Marcelino-Guimaraes, F.C. (2016). Plant Small Heat Shock Proteins and Its Interactions with Biotic Stress. In: Heat Shock Proteins and Plants: Springer. 19-39.
Lu, Z., and Cyr, D.M. (1998). The conserved carboxyl terminus and zinc finger-like domain of the co-chaperone Ydj1 assist Hsp70 in protein folding. Journal of Biological Chemistry 273:5970-5978.
Ma, W., Zhao, T., Li, J., Liu, B., Fang, L., Hu, Y., and Zhang, T. (2016). Identification and characterization of the GhHsp20 gene family in Gossypium hirsutum. Scientific reports 6:32517.
Marrs, K.A., Casey, E.S., Capitant, S.A., Bouchard, R.A., Dietrich, P.S., Mettler, I.J., and Sinibaldi, R.M. (1993). Characterization of two maize HSP90 heat shock protein genes: expression during heat shock, embryogenesis, and pollen development. genesis 14:27-41.
Mayer, M.P., and Bukau, B. (1999). Molecular chaperones: the busy life of Hsp90. Current Biology 9:R322-R325.
Mchaourab, H.S., Godar, J.A., and Stewart, P.L. (2009). Structure and mechanism of protein stability sensors: chaperone activity of small heat shock proteins. Biochemistry 48:3828-3837.
McLaughlin, S.H., Smith, H.W., and Jackson, S.E. (2002). Stimulation of the weak ATPase activity of human hsp90 by a client protein. Journal of molecular biology 315:787-798.
Miernyk, J.A. (2001). The J-domain proteins of Arabidopsis thaliana: an unexpectedly large and diverse family of chaperones. Cell stress & chaperones 6:209-218.
Mogk, A., Tomoyasu, T., Goloubinoff, P., Rüdiger, S., Röder, D., Langen, H., and Bukau, B. (1999). Identification of thermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpB. The EMBO journal 18:6934-6949.
Muench, D.G., Wu, Y., Zhang, Y., Li, X., Boston, R.S., and Okita, T.W. (1997). Molecular cloning, expression and subcellular localization of a BiP homolog from rice endosperm tissue. Plant and Cell Physiology 38:404-412.
Muthusamy, S.K., Dalal, M., Chinnusamy, V., and Bansal, K.C. (2017). Genome-wide identification and analysis of biotic and abiotic stress regulation of small heat shock protein (HSP20) family genes in bread wheat. Journal of Plant Physiology 211:100-113.
Nakamoto, H., and Vigh, L. (2007). The small heat shock proteins and their clients. Cellular and Molecular Life Sciences 64:294-306.
Ouyang, Y., Chen, J., Xie, W., Wang, L., and Zhang, Q. (2009). Comprehensive sequence and expression profile analysis of Hsp20 gene family in rice. Plant molecular biology 70:341-357.
Pandey, B., Kaur, A., Gupta, O.P., Sharma, I., and Sharma, P. (2015). Identification of HSP20 gene family in wheat and barley and their differential expression profiling under heat stress. Applied biochemistry and biotechnology 175:2427-2446.
Park, S.J., Borin, B.N., Martinez-Yamout, M.A., and Dyson, H.J. (2011). The client protein p53 adopts a molten globule–like state in the presence of Hsp90. Nature Structural and Molecular Biology 18:537.
Parsell, D., and Lindquist, S. (1993). The function of heat-shock proteins in stress tolerance: degradation and reactivation of damaged proteins. Annual review of genetics 27:437-496.
Pearl, L.H., and Prodromou, C. (2006). Structure and mechanism of the Hsp90 molecular chaperone machinery. Annu. Rev. Biochem. 75:271-294.
Picard, D. (2002). Heat-shock protein 90, a chaperone for folding and regulation. Cellular and Molecular Life Sciences 59:1640-1648.
Prodromou, C., Siligardi, G., O'Brien, R., Woolfson, D.N., Regan, L., Panaretou, B., Ladbury, J.E., Piper, P.W., and Pearl, L.H. (1999). Regulation of Hsp90 ATPase activity by tetratricopeptide repeat (TPR)‐domain co‐chaperones. The EMBO journal 18:754-762.
Queitsch, C., Hong, S.-W., Vierling, E., and Lindquist, S. (2000). Heat shock protein 101 plays a crucial role in thermotolerance in Arabidopsis. The Plant Cell 12:479-492.
Queitsch, C., Sangster, T.A., and Lindquist, S. (2002). Hsp90 as a capacitor of phenotypic variation. Nature 417:618-624.
Ryan, M.T., and Pfanner, N. (2001). Hsp70 proteins in protein translocation. Advances in protein chemistry 59:223-242.
Sable, A., Rai, K.M., Choudhary, A., Yadav, V.K., Agarwal, S.K., and Sawant, S.V. (2018). Inhibition of Heat Shock proteins HSP90 and HSP70 induce oxidative stress, suppressing cotton fiber development. Scientific Reports 8:3620.
Sanchez, Y., and Lindquist, S.L. (1990). HSP104 required for induced thermotolerance. Science 248:1112.
Sarkar, N.K., Kim, Y.-K., and Grover, A. (2009). Rice sHsp genes: genomic organization and expression profiling under stress and development. BMC genomics 10:393.
Sarkar, N.K., Kundnani, P., and Grover, A. (2013a). Functional analysis of Hsp70 superfamily proteins of rice (Oryza sativa). Cell Stress and Chaperones 18:427-437.
Sarkar, N.K., Thapar, U., Kundnani, P., Panwar, P., and Grover, A. (2013b). Functional relevance of J-protein family of rice (Oryza sativa). Cell Stress and Chaperones 18:321-331.
Scharf, K.-D., Siddique, M., and Vierling, E. (2001). The expanding family of Arabidopsis thaliana small heat stress proteins and a new family of proteins containing α-crystallin domains (Acd proteins). Cell stress & chaperones 6:225-237.
Schirmer, E.C., Homann, O.R., Kowal, A.S., and Lindquist, S. (2004). Dominant gain-of-function mutations in Hsp104p reveal crucial roles for the middle region. Molecular biology of the cell 15:2061-2072.
Shafikova, T., Omelichkina, Y.V., Soldatenko, A., Enikeev, A., Kopytina, T., Rusaleva, T., and Volkova, O. (2013). Tobacco cell cultures transformed by the hsp101 gene exhibit an increased resistance to Clavibacter michiganensis ssp. sepedonicus. In: Doklady Biological Sciences: Springer. 165-167.
Shi, L.-X., and Theg, S.M. (2010). A stromal heat shock protein 70 system functions in protein import into chloroplasts in the moss Physcomitrella patens. The Plant Cell 22:205-220.
Siligardi, G., Panaretou, B., Meyer, P., Singh, S., Woolfson, D.N., Piper, P.W., Pearl, L.H., and Prodromou, C. (2002). Regulation of Hsp90 ATPase activity by the co-chaperone Cdc37p/p50 cdc37. Journal of Biological Chemistry 277:20151-20159.
Silva, J.C., Borges, J.C., Cyr, D.M., Ramos, C.H., and Torriani, I.L. (2011). Central domain deletions affect the SAXS solution structure and function of Yeast Hsp40 proteins Sis1 and Ydj1. BMC structural biology 11:40.
Singh, A., Singh, U., Mittal, D., and Grover, A. (2010). Genome-wide analysis of rice ClpB/HSP100, ClpC and ClpD genes. BMC genomics 11:95.
Song, H., Zhao, R., Fan, P., Wang, X., Chen, X., and Li, Y. (2009). Overexpression of AtHsp90. 2, AtHsp90. 5 and AtHsp90. 7 in Arabidopsis thaliana enhances plant sensitivity to salt and drought stresses. Planta 229:955-964.
Su, P.-H., and Li, H.-m. (2010). Stromal Hsp70 is important for protein translocation into pea and Arabidopsis chloroplasts. The Plant Cell 22:1516-1531.
Sung, D.Y., Vierling, E., and Guy, C.L. (2001). Comprehensive expression profile analysis of the Arabidopsis Hsp70 gene family. Plant physiology 126:789-800.
Takayama, S., Bimston, D.N., Matsuzawa, S.i., Freeman, B.C., Aime‐Sempe, C., Xie, Z., Morimoto, R.I., and Reed, J.C. (1997). BAG‐1 modulates the chaperone activity of Hsp70/Hsc70. The EMBO journal 16:4887-4896.
Tang, T., Yu, A., Li, P., Yang, H., Liu, G., and Liu, L. (2016). Sequence analysis of the Hsp70 family in moss and evaluation of their functions in abiotic stress responses. Scientific reports 6.
Tyedmers, J., Mogk, A., and Bukau, B. (2010). Cellular strategies for controlling protein aggregation. Nature reviews Molecular cell biology 11:777-788.
Vierling, E. (1991). The roles of heat shock proteins in plants. Annual review of plant biology 42:579-620.
Wang, G., Cai, G., Kong, F., Deng, Y., Ma, N., and Meng, Q. (2014). Overexpression of tomato chloroplast-targeted DnaJ protein enhances tolerance to drought stress and resistance to Pseudomonas solanacearum in transgenic tobacco. Plant Physiology and Biochemistry 82:95-104.
Wang, H., Goffreda, M., and Leustek, T. (1993). Characteristics of an Hsp70 homolog localized in higher plant chloroplasts that is similar to DnaK, the Hsp70 of prokaryotes. Plant physiology 102:843-850.
Wang, W., Vinocur, B., Shoseyov, O., and Altman, A. (2004). Role of plant heat-shock proteins and molecular chaperones in the abiotic stress response. Trends in plant science 9:244-252.
Waters, E.R. (2012). The evolution, function, structure, and expression of the plant sHSPs. Journal of experimental botany 64:391-403.
Waters, E.R., and Rioflorido, I. (2007). Evolutionary analysis of the small heat shock proteins in five complete algal genomes. Journal of Molecular Evolution 65:162-174.
Wegele, H., Müller, L., and Buchner, J. (2004). Hsp70 and Hsp90—a relay team for protein folding. In: Reviews of physiology, biochemistry and pharmacology: Springer. 1-44.
Wen, F., Wu, X., Li, T., Jia, M., Liu, X., Li, P., Zhou, X., Ji, X., and Yue, X. (2017). Genome-wide survey of heat shock factors and heat shock protein 70s and their regulatory network under abiotic stresses in Brachypodium distachyon. PloS one 12:e0180352.
Xu, Z.-S., Li, Z.-Y., Chen, Y., Chen, M., Li, L.-C., and Ma, Y.-Z. (2012). Heat shock protein 90 in plants: molecular mechanisms and roles in stress responses. International journal of molecular sciences 13:15706-15723.
Yan, H., Zhang, A., Chen, J., He, X., Xu, B., Xie, G., Miao, Z., Zhang, X., and Huang, L. (2017). Genome-Wide Analysis of the PvHsp20 Family in Switchgrass: Motif, Genomic Organization, and Identification of Stress or Developmental-Related Hsp20s. Frontiers in plant science 8:1024.
Young, J.C., Moarefi, I., and Hartl, F.U. (2001). Hsp90. J Cell Biol 154:267-274.
Yu, J., Cheng, Y., Feng, K., Ruan, M., Ye, Q., Wang, R., Li, Z., Zhou, G., Yao, Z., and Yang, Y. (2016). Genome-wide identification and expression profiling of tomato Hsp20 gene family in response to biotic and abiotic stresses. Frontiers in plant science 7.
Zhang, J., Li, J., Liu, B., Zhang, L., Chen, J., and Lu, M. (2013). Genome-wide analysis of the Populus Hsp90 gene family reveals differential expression patterns, localization, and heat stress responses. BMC genomics 14:532.
Zhang, J., Liu, B., Li, J., Zhang, L., Wang, Y., Zheng, H., Lu, M., and Chen, J. (2015a). Hsf and Hsp gene families in Populus: genome-wide identification, organization and correlated expression during development and in stress responses. BMC genomics 16:181.
Zhang, L., Zhao, H.-K., Dong, Q.-L., Zhang, Y.-Y., Wang, Y.-M., Li, H.-Y., Xing, G.-J., Li, Q.-Y., and Dong, Y.-S. (2015b). Genome-wide analysis and expression profiling under heat and drought treatments of HSP70 gene family in soybean (Glycine max L.). Frontiers in plant science 6.
Zhichang, Z., Wanrong, Z., Jinping, Y., Jianjun, Z., Xufeng, L.Z.L., and Yang, Y. (2010). Over-expression of Arabidopsis DnaJ (Hsp40) contributes to NaCl-stress tolerance. African Journal of Biotechnology 9:972-978.
How to Cite
Sable, A., & Agarwal, S. (2018, March 31). Plant Heat Shock Protein Families: Essential Machinery for Development and Defense. Journal of Biological Sciences and Medicine, 4(1). Retrieved from
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