Os12g0569700

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OsHsp23.7 is a member of Heat shock proteins(Hsps), it belongs to HSP70 family[1][2].

Annotated Information

Function

Figure 1.Drought tolerance assays of OsHsp23.7-OE transgenic rice(from reference [1]).
Figure 2.Salt tolerance assays of OsHsp23.7-OE transgenic rice(from reference [1]).

Both OsHsp17.0-OE and OsHsp23.7-OE transgenic lines demonstrated higher germination ability compared to wild-type (WT) plants when subjected to mannitol and NaCl. Phenotypic analysis showed that transgenic rice lines displayed a higher tolerance to drought and salt stress compared to WT plants. In addition, transgenic rice lines showed significantly lower REC, lower MDA content and higher free proline content than WT under drought and salt stresses. These results suggest that OsHsp17.0 and OsHsp23.7 play an important role in rice acclimation to salt and drought stresses and are useful for engineering drought and salt tolerance rice[1].

GO assignment(s): GO:0005524

Mutation

Figure 3.Gene tree of the nine rice HSPs(from reference [2]).
  • The expression of OsHsp17.0 and OsHsp23.7 in transgenic lines (T2 generation) was checked by real-time qPCR. Three highly

over-expressed lines were identified in the OsHsp17.0-OE and OsHsp23.7-OE lines respectively (Fig. 1A) and were used for later characterization.

  • Three-week-old seedlings were exposed to air for 9.5 h, and then were transferred to normal hydroponic conditions and recovered for 10 d.(Figure 1D) Seedlings before treatment. (Figure 1E) Seedlings were exposed to air for 9.5 h. (Figure 1F) Seedlings were transferred to normal hydroponic conditions and recovered for 10 d.
  • Three-week-old seedlings were watered with 200 mM NaCl solution for 24 h and then were transferred to normal hydroponic conditions and recovered for 10 d. (Figure 2D) Seedlings before treatment. (Figure 2E) Seedlings were subjected to 200 mM NaCl solution for

24 h. (Figure 2F) Seedlings were transferred to normal hydroponic conditions and recovered for 10 d.

Expression

  • Overexpression of OsHsp17.0 and OsHsp23.7 enhanced drought tolerance and salt tolerance.
  • After temperature treatment, leaf tips of both transgenic plants and WT plants were rolled or withered, no significant differences were observed between them. After recovery for 7 d, both transgenic plants and WT plants remained alive and produced new leaves.
  • There were no significant differences in content of MDA content and proline content between WT and OE lines under normal conditions. However, after stress treatments (20%PEG6000, 200 mM NaCl, 45℃ and 5℃), the MDA content was significantly higher in WT than in OE lines. The accumulation of proline in OE plants was significantly more than that in WT plants, which suggesting that less membrane damage and improved osmotic adjustment ability in transgenic OE plants under stresses.
Primer[1] Forward primer Reverse primer
PCR-amplifie 5'-CGGGATCCCACCCAACTCTTCTTCTTCC-3' 5'-GCTCTAGACTTGACCTTGACAAACTCCC-3'
5'-CGGGATCCATGAGCCTACTGCTGCT-3' 5'-AATCTAGATCGTACACCTGGATCAACA-3'
real-time quantitative PCR 5'-AAGGTGGACCAGGTGAAGG-3' 5'-GACCTTGACAAACTCCCGTT-3'
5'-AGACCACCCACCATTGAGATT-3' 5'-GCCACCAACAAGGATGAACAT-3'
5'-GGAAGTAAGGAAGGAGGAGGAA-3' 5'-CAGAGGTGATGCTAAGGTGTTC-3'

Evolution

Gene tree were conducted using the software Molecular Evolutionary Genetics Analysis (MEGA) Version 4.0 by the neighbor-joining method with pairwise deletion and the Poisson correction model.As shown in Figure 1, based on amino acids sequence homology, nine OsHSP genes were divided into three classes, among them OsHSP80.2, OsHSP74.8 and OsHSP50.2 belong to HSP90 family; OsHSP71.1, OsHSP58.7 and OsHSP23.7 belong to HSP70 family; OsHSP26.7, OsHSP24.1 and OsHSP17.0 belong to sHSP family[2].

Knowledge Extension

Heat shock proteins (Hsps) belong to a class of proteins that are conserved in prokaryotes and eukaryotes and are especially abundant in plants. Hsps are highly expressed in plants and other organisms after being stimulated by high temperature and other stresses. The sHsps are much more abundant in higher plants than in other organisms[3]. Expression of nine OsHSP genes was affected differentially by abiotic stresses and abscisic acid (ABA). All nine OsHSP genes were induced strongly by heat shock treatment, whereas none of them were induced by cold. The transcripts of OsHSP80.2, OsHSP71.1 and OsHSP23.7 were increased during salt tress treatment. Expression of OsHSP80.2 and OsHSP24.1 genes were enhanced while treated with 10% PEG. Only OsHSP71.1 was induced by ABA while OsHSP24.1 was suppressed by ABA. These observations imply that the nine OsHSP genes may play different roles in plant development and abiotic stress responses[2]. According to their approximate molecular weights, HSPs are grouped into five families: HSP100s, HSP90s, HSP70s, HSP60s and sHSPs (small HSPs, o40 kDa)[4]. Most HSPs function as molecular chaperones in maintaining homeostasis of protein folding and are thought to be responsible for the acquisition of thermo tolerance[3]. It is believed that the accumulations of HSPs play a pivotal role in abiotic stress.

Labs working on this gene

  • Hunan Provincial Key Laboratory for Germplasm Innovation and Utilization of Crop, Hunan Agricultural University, Changsha 410128, China
  • College of Bioscience and Biotechnology, Hunan Agricultural University, Changsha 410128, China
  • Crop Gene Engineering Key Laboratory of Hunan Province, Hunan Agricultural University, Changsha 410128, China

References

  1. 1.0 1.1 1.2 1.3 1.4 Zou J, Liu C, Liu A, et al. Overexpression of< i> OsHsp17. 0</i> and< i> OsHsp23. 7</i> enhances drought and salt tolerance in rice[J]. Journal of plant physiology, 2012, 169(6): 628-635.
  2. 2.0 2.1 2.2 2.3 Zou J, Liu A, Chen X, et al. Expression analysis of nine rice heat shock protein genes under abiotic stresses and ABA treatment[J]. Journal of plant physiology, 2009, 166(8): 851-861.
  3. 3.0 3.1 Vierling E. The roles of heat shock proteins in plants[J]. Annual review of plant biology, 1991, 42(1): 579-620.
  4. Trent J D. A review of acquired thermotolerance, heat‐shock proteins, and molecular chaperones in archaea[J]. FEMS microbiology reviews, 1996, 18(2‐3): 249-258.

Structured Information