Molecular characterization, expression pattern and function analysis of theOsHSP90family in rice

Abstract

The HSP90 is an abundant chaperone protein that is conserved in all eukaryotes. The main function of HSP90 is to assist other proteins to fold properly. In this study, we uncovered and analysed nine OsHSP90 (OsHSP90-1-OsHSP90-9) family members in rice Nipponbare, in which three distinct motifs were identified. All the HSP90 proteins were classified into three major groups (I, II, III) by phylogenetic analysis. The expression of OsHSP90 family in 10 tissues was examined by real-time polymerase chain reaction (PCR). OsHSP90-4, OsHSP90-6 and OsHSP90-7 had high expression, while OsHSP90-5 and OsHSP90-8 had very low expression across almost all 10 samples. The gene that encodes OsHSP90-1 was preferentially expressed in embryo at 14 days after flowering. It has been reported that some heat shock proteins were up-regulated in response to heat or other stresses. However, in our study the expression pattern of OsHSP90 genes is heterogeneous under a range of stress conditions. The expression of OsHSP90-2 and OsHSP90-4 was up-regulated under drought, salt, cold and heat conditions, while the expression of OsHSP90-3 and OsHSP90-5 was downregulated under salt and drought conditions. OsHSP90-7 and OsHSP90-9 were down-regulated only under drought conditions. OsHSP90-6 did not change its expression across all conditions compared to control. Overexpression of OsHSP90-2 in E. coli could enhance cell viability and significantly improved resistance to heat, high salinity and drought stress conditions. The results presented here may provide new insights into the function of OsHSP90 family in rice.

Intensive herbicide use has selected for constitutively elevated levels of stress‐responsive mRNAs and proteins in multiple herbicide‐resistant Avena fatua L

“…Heat shock proteins (Hsps) and the diverse families of small Hsps in plants are known to be induced or repressed in response to biotic and abiotic stresses . In addition to their roles as molecular chaperones that prevent protein misfolding, some Hsps regulate TFs for a diverse set of genes, and several Hsps are involved in adaptation of Saccharomyces cerevisiae to the auxinic herbicide 2,4‐D .…”

“…wileyonlinelibrary.com/journal/ps Heat shock proteins (Hsps) and the diverse families of small Hsps in plants are known to be induced or repressed in response to biotic and abiotic stresses. 94,95 In addition to their roles as molecular chaperones that prevent protein misfolding, some Hsps regulate TFs for a diverse set of genes, 96 and several Hsps are involved in adaptation of Saccharomyces cerevisiae to the auxinic herbicide 2,4-D. 97 In A. fatua, we observed constitutive reduction of three Hsp DEGs (5629.3793, 5629.2548 and 7001.7) and one Hsp protein (spot 797) in MHR4 A. fatua (Tables 3 and 4). The functionally related DEG 4994 (cyclophilin-like peptidylprolyl isomerase), which catalyzes a rate-limiting step in protein folding, 98 was also constitutively reduced in MHR4 plants.…”

The heat‐shock protein/chaperone network and multiple stress resistance

“…In rice, OsAHL1 was shown to directly induce HSP101 and HSP90 expression leading to drought resistance (Zhou et al, 2016). OsHSP90-2 and OsHSP90-4 were also found up-regulated after drought, cold, heat and salt stresses (Zhang et al, 2016). When introduced in E. coli, OsHSP90-2 was sufficient to induce resistance to heat, high salinity and drought (Zhang et al, 2016).…”

“…OsHSP90‐2 and OsHSP90‐4 were also found up‐regulated after drought, cold, heat and salt stresses (Zhang et al ., ). When introduced in E. coli , OsHSP90‐2 was sufficient to induce resistance to heat, high salinity and drought (Zhang et al ., ). A similar modulation of HSFs and HSPs was found in tomato in response to heat, drought and salinity (Fragkostefanakis et al ., ).…”

Molecular characterisation and function analysis of the rice OsDUF872 family

“…At present, the specific mechanism by which heat tolerance is enhanced in E. coli recombinants transformed with OsDUF872.2 remains unclear. It has been reported that the overexpression of some heat shock protein genes can enhance the heat tolerance in E. coli [39][40][41][42]. Under heat conditions, it is possible that OsDUF872.2 interacts with some heat shock protein, and the proteinprotein interaction can lead to improve the heat stress resistance in transgenic E. coli.…”