Expression of a gene encoding a 16.9-kDa heat-shock protein, Oshsp16.9, in
            <i>Escherichia coli</i>
            enhances thermotolerance

Yeh, Ching-Hui; Chang, Pi-Fang Linda; Yeh, Kai‐Wun; Lin, Wen‐Chi; Chen, Yih-Ming; Lin, Ching‐Fuh

doi:10.1073/pnas.94.20.10967

Cited by 129 publications

(96 citation statements)

References 39 publications

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“…Transgenic potato plants expressing DcHSP17.7 exhibited enhanced cellular membrane stability and tuberization in vitro at elevated temperatures, compared with wild type and vector controls. Some smHSP genes from plants have been introduced into E. coli or other plant species, and enhanced thermotolerance in transgenic lines has been reported: expression of either a gene encoding rice 16.9 kDa HSP (Yeh et al 1995(Yeh et al , 1997 or a chestnut HSP17.5 (Soto et al 1999) enhanced cell viability in E. coli. Introduction of a DcHSP17.7 gene into E. coli also resulted in increased survival rates of cells at elevated temperatures (T.E.…”

Section: Discussionmentioning

confidence: 99%

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Introduction of the carrot HSP17.7 into potato (Solanum tuberosum L.) enhances cellular membrane stability and tuberization in vitro

Ahn

Zimmerman

2005

Plant Cell & Environment

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We have examined the ability of a carrot (Daucus carota L.) heat shock protein gene encoding HSP17.7 (DcHSP17.7) to confer enhanced heat tolerance to potato (Solanum tuberosum L.), a cool‐season crop. The DcHSP17.7 gene was fused to a 6XHistidine (His) tag to distinguish the engineered protein from endogenous potato proteins and was introduced into the potato cultivar ‘Désirée’ under the control of the cauliflower mosaic virus (CaMV) 35S promoter. Western analysis showed that engineered DcHSP17.7 was constitutively, but not abundantly, expressed in transgenic potato lines before heat stress. Leaves from multiple regenerated potato lines that contain the transgene exhibited significantly improved cellular membrane stability at high temperatures, compared with wild‐type and vector control plants. Transgenic potato lines also exhibited enhanced tuberization in vitro: under a condition of constant heat stress, at 29 °C, nodal sections of the transgenic lines produced larger and heavier microtubers at higher rates, compared to the wild type and vector controls. The dry weight and percentages of microtubers that were longer than 5 mm were up to three times higher in the transgenic lines. Our results suggest that constitutive expression of carrot HSP17.7 can enhance thermotolerance in transgenic potato plants. To our knowledge, this is the first study that shows that the thermotolerance of potato can be enhanced through gene transfer.

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Section: Discussionmentioning

confidence: 99%

“…Overexpression of either a gene encoding rice 16.9 kDa HSP (Yeh et al . 1995(Yeh et al . , 1997 or a gene encoding chestnut HSP17.5 (Soto et al .…”

Section: Introductionmentioning

confidence: 99%

Introduction of the carrot HSP17.7 into potato (Solanum tuberosum L.) enhances cellular membrane stability and tuberization in vitro

Ahn

Zimmerman

2005

Plant Cell & Environment

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“…Of these, members of the CI subfamily, like Hsp16.9A (Chen et al 2014), Hsp18.0 (Guan et al 2004), Hsp18.0 of the CII subfamily (Chang et al 2007) and the chloroplast-localised Hsp26.7 (Lee et al 2000) have been investigated. Overexpression of rice Hsp16.9 (CI subfamily) in Escherichia coli conferred thermo-tolerance to the bacteria at temperatures that were otherwise considered lethal (Yeh et al 1997). Transgenic rice lines that overexpressed Hsp17.7 (CI subfamily) displayed higher drought tolerance than the untransformed plants (Sato and Yokoya, 2008).…”

Section: Introductionmentioning

confidence: 99%

Characterization of rice small heat shock proteins targeted to different cellular organelles

Mani

Ramakrishna

Suguna

2015

Cell Stress and Chaperones

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Small heat shock proteins (sHSPs) are a family of ATP-independent molecular chaperones which prevent cellular protein aggregation by binding to misfolded proteins. sHSPs form large oligomers that undergo drastic rearrangement/dissociation in order to execute their chaperone activity in protecting substrates from stress. Substrate-binding sites on sHSPs have been predominantly mapped on their intrinsically disordered N-terminal arms. This region is highly variable in sequence and length across species, and has been implicated in both oligomer formation and in mediating chaperone activity. Here, we present our results on the functional and structural characterization of five sHSPs in rice, each differing in their subcellular localisation, viz., cytoplasm, nucleus, chloroplast, mitochondria and peroxisome. We performed activity assays and dynamic light scattering studies to highlight differences in the chaperone activity and quaternary assembly of sHSPs targeted to various organelles. By cloning constructs that differ in the length and sequence of the tag in the N-terminal region, we have probed the sensitivity of sHSP oligomer assembly and chaperone activity to the length and amino acid composition of the N-terminus. In particular, we have shown that the incorporation of an N-terminal tag has significant consequences on sHSP quaternary structure.

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“…Studies of two point mutations of OsHsp16.9, GST-N74E73K and GST-N74E74K, indicated that amino acid residues 73 and 74 are an important part of the substrate-binding site of OsHsp16.9. Yeh et al (1997) introduced Oshsp16.9 in E. coli using the pGEX-2T expression vector to analyze the possible function of this sHsp under heat stress. The survivability of E. coli XL1-blue cells transformed with a recombinant plasmid containing glutathione Stransferase (GST)-OsHsp16.9 fusion protein (pGST-FL cells) was compared with the control E. coli cells (transformed with the pGEX-2T vector; pGST cells) under HS.…”

Section: High Temperature Tolerant Transgenics Raised Through Alterinmentioning

confidence: 99%

“…Hsps reportedly function as molecular chaperones that co-operate as a functional-network in protecting cells against damage due to HS. Hsp16.9, Hsp17.1, Hsp17.3 and Hsp18.1 are shown to prevent the aggregation or denaturation of proteins during HS (Lee et al, 1995;Yeh et al, 1997;Young et al, 1999;Low et al, 2000). Hsp100 is shown to rescue the heat-induced protein aggregates by their re-solubilization during the recovery phase (Glover and Lindquist, 1998).…”

Section: Synthesis To Propose a Modelmentioning

confidence: 99%

Genetic engineering for heat tolerance in plants

Singh

Grover

2008

Physiol Mol Biol Plants

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High temperature tolerance has been genetically engineered in plants mainly by over-expressing the heat shock protein genes or indirectly by altering levels of heat shock transcription factor proteins. Apart from heat shock proteins, thermotolerance has also been altered by elevating levels of osmolytes, increasing levels of cell detoxification enzymes and through altering membrane fluidity. It is suggested that Hsps may be directly implicated in thermotolerance as agents that minimize damage to cell proteins. The other three above approaches leading to thermotolerance in transgenic experiments though operate in their own specific ways but indirectly might be aiding in creation of more reductive and energy-rich cellular environment, thereby minimizing the accumulation of damaged proteins. Intervention in protein metabolism such that accumulation of damaged proteins is minimized thus appears to be the main target for genetically-engineering crops against high temperature stress. High temperature-induced gene expression system is one of the best-studied model systems for analyzing induced gene expression. The molecular basis of heat shock (HS) response was revealed for the first time when Ritossa (1962) reported that temperature elevation brings about altered puffing pattern of polytene chromosomes in Drosophila. Tissieres et al. (1974) for the first time showed that the HS condition results in altered protein profile in the Drosophila cells. Further studies established that nearly all organisms, ranging from bacteria to man, respond to HS by synthesizing a new set of proteins called heat shock proteins (Hsp). The HS system has been investigated in great depth using diverse biological systems including microbes (e.g. Escherichia coli, Saccharomyces cerevisiae), animals (e.g. Drosophila melanogaster, Homo sapiens) and plants (e.g. Arabidopsis thaliana, Oryza sativa, Solanum lycopersicon) species. In recent years, detailed understanding has been gained on various components of the heat shock response (HSR) in living organisms including features like heat shock genes/proteins, heat shock promoters and heat shock elements (HSEs), heat shock factors (HSFs), possible receptors of the heat shock response, signaling components and chromatin remodeling aspects (Grover, 2002, Wahid et al., 2007.Plant scientists have a concern in altering the HS response as high ambient temperature is one of the major constraints in obtaining maximum output from the crop plants. Most crops are affected by daily fluctuations in high day and/or night temperatures. While some stages of plant growth may be more sensitive to high temperature than others, there is an overall reduction in plant performance when temperature is higher than the optimal temperature at specific growth stages. Conventional breeding for high temperature stress tolerance has not been much successful due to several reasons like lack of suitable source of genes in sexuallycompatible gene pools, complex nature of the HS trait, lack of understanding on the genetic mech...

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Expression of a gene encoding a 16.9-kDa heat-shock protein, Oshsp16.9, in Escherichia coli enhances thermotolerance

Abstract: A gene encoding the rice 16.9-kDa class I low-molecular-mass (LMM) heat-shock protein (HSP), Oshsp16.9, was introduced into Escherichia coli using the

Cited by 129 publications

References 39 publications

Introduction of the carrot HSP17.7 into potato (Solanum tuberosum L.) enhances cellular membrane stability and tuberization in vitro

Introduction of the carrot HSP17.7 into potato (Solanum tuberosum L.) enhances cellular membrane stability and tuberization in vitro

Characterization of rice small heat shock proteins targeted to different cellular organelles

Genetic engineering for heat tolerance in plants

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