ZmHSP16.9, a cytosolic class I small heat shock protein in maize (Zea mays), confers heat tolerance in transgenic tobacco

Sun, Lingyu; Liu, Yang; Kong, Xiangpei; Zhang, Dan; Pan, Junxiao; Zhou, Yan; Wang, Li; Li, Dequan; Yang, Xinghong

doi:10.1007/s00299-012-1262-8

Cited by 115 publications

(82 citation statements)

References 45 publications

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“…Despite the apparent requirement of both CI and CII HSPs for optimal heat tolerance, as demonstrated by the RNAi experiments, constitutive expression of either class alone enhanced the greening of dark-grown seedlings after direct heat stress (basal thermotolerance), consistent with previous reports using different assays to test the heat stress tolerance of plants constitutively expressing CI or CII sHSPs (Sun et al, 2012;Zhou et al, 2012;Wang et al, 2015). We also observed that, even though endogenous sHSPs are highly expressed in heat-acclimated plants, the individual sHSP OE lines had a still higher survival rate than the wild type after heat stress following acclimation.…”

Section: Discussionsupporting

confidence: 90%

“…However, only single alleles were tested, and no complementation experiments were performed. Further evidence for the stress-protective role of CI and CII sHSPs in plants has primarily involved constitutive expression or overexpression of a single sHSP in different plant species, including Arabidopsis, rice (Oryza sativa), maize (Zea mays), and carrot (Daucus carota), as well as others (Malik et al, 1999;Ahn and Zimmerman, 2006;Jiang et al, 2009;Sun et al, 2012;Zhou et al, 2012;Mu et al, 2013;Wang et al, 2015). A very restricted set of stress-resistant phenotypes has been reported for sHSP-overexpressing transgenic materials, and these studies have not provided mechanistic insight into sHSP function or distinguished differences between CI and CII sHSPs.…”

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confidence: 99%

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Class I and II small heat-shock proteins protect protein translation factors during heat stress

et al. 2016

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The ubiquitous small heat shock proteins (sHSPs) are well documented to act in vitro as molecular chaperones to prevent the irreversible aggregation of heat-sensitive proteins. However, the in vivo activities of sHSPs remain unclear. To investigate the two most abundant classes of plant cytosolic sHSPs (class I [CI] and class II [CII]), RNA interference (RNAi) and overexpression lines were created in Arabidopsis (Arabidopsis thaliana) and shown to have reduced and enhanced tolerance, respectively, to extreme heat stress. Affinity purification of CI and CII sHSPs from heat-stressed seedlings recovered eukaryotic translation elongation factor (eEF) 1B (a-, b-, and g-subunits) and eukaryotic translation initiation factor 4A (three isoforms), although the association with CI sHSPs was stronger and additional proteins involved in translation were recovered with CI sHSPs. eEF1B subunits became partially insoluble during heat stress and, in the CI and CII RNAi lines, showed reduced recovery to the soluble cell fraction after heat stress, which was also dependent on HSP101. Furthermore, after heat stress, CI sHSPs showed increased retention in the insoluble fraction in the CII RNAi line and vice versa. Immunolocalization revealed that both CI and CII sHSPs were present in cytosolic foci, some of which colocalized with HSP101 and with eEF1Bg and eEF1Bb. Thus, CI and CII sHSPs have both unique and overlapping functions and act either directly or indirectly to protect specific translation factors in cytosolic stress granules.

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Section: Discussionsupporting

confidence: 90%

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confidence: 99%

Class I and II small heat-shock proteins protect protein translation factors during heat stress

et al. 2016

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“…According to Sun et al (2012), water stress induces heat-resistant protein expression, such as HSP. Ristic et al (1991) found a HSP band of approximately 45 kDa in maize leaves from a heat and water stress-tolerant line.…”

Section: Discussionmentioning

confidence: 99%

Heat-resistant protein expression during germination of maize seeds under water stress

Abreu¹,

Neta²,

Pinho³

et al. 2016

Genet. Mol. Res.

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ABSTRACT. Low water availability is one of the factors that limit agricultural crop development, and hence the development of genotypes with increased water stress tolerance is a challenge in plant breeding programs. Heat-resistant proteins have been widely studied, and are reported to participate in various developmental processes and to accumulate in response to stress. This study aimed to evaluate heat-resistant protein expression under water stress conditions during the germination of maize seed inbreed lines differing in their water stress tolerance. Maize seed lines 91 and 64 were soaked in 0, -0.3, -0.6, and -0.9 MPa water potential for 0, 6, 12, 18, and 24 h. Line 91 is considered more water stress-tolerant than line 64. The analysis of heat-resistant protein expression was made by gel electrophoresis and spectrophotometry. In general, higher expression of heat-resistant proteins was observed in seeds from line 64 subjected to shorter soaking periods and lower water potentials. However, in the water stress-tolerant line 91, a higher expression was observed in seeds that were subjected to -0.3 and -0.6 MPa water potentials. In the absence of water stress, heat-resistant protein expression was reduced with increasing soaking period. Thus, there was a difference in heat-resistant protein expression among the seed lines differing in water stress tolerance. Increased heatresistant protein expression was observed in seeds from line 91 when subjected to water stress conditions for longer soaking periods.

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“…In Arabidopsis, 8 Hsp100 members (Agarwal et al, 2001), 7 Hsp90 members (Krishna and Gloor, 2001), 18 Hsp70 members (Lin et al, 2001), 11 Hsp60 members (Hill and Hemmingsen, 2001), and 13 sHsps members (Scharf et al, 2001) have been identified in the genome and analyzed. Hsps from different families have been also reported in other plant species, such as cereals (Maestri et al, 2002), maize (Sun et al, 2012), and wheat (Kumar et al, 2012). Modifying the expression of Hsp via genetic engineering has been shown to be useful for enhancing temperature stress tolerance in plants.…”

Section: Introductionmentioning

confidence: 93%

Identification of heat shock proteins via transcriptome profiling of tree peony leaf exposed to high temperature

Zhang¹,

Cheng²,

Ya³

et al. 2015

Genet. Mol. Res.

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ABSTRACT. The tree peony leaf is an important vegetative organ that is sensitive to abiotic stress and particularly to high temperature. This sensitivity affects plant growth and restricts tree peony distribution. However, the transcriptomic information currently available on the peony leaf in public databases is limited. In this study, we sequenced the transcriptomes of peony leaves subjected to high temperature using the Illumina HiSeq TM 2000 platform. We performed de novo assembly of 93,714 unigenes (average length of 639.7 bp). By searching the public databases, 22,323 unigenes and 13,107 unigenes showed significant similarities with proteins in the NCBI non-redundant protein database and SWISS-PROT database (E-value < 1e-5), respectively. We assigned 17,340 unigenes to Gene Ontology categories, and we assigned 7618 unigenes to clusters of orthologous groups for eukaryotic complete genomes. By searching the Kyoto Encyclopedia of Genes and Genomes Pathway database, 8014 unigenes were assigned to 6 main categories, including 290 KEGG pathways. To advance research on improving thermotolerance, we identified 24 potential heat shock protein genes with complete open reading frames from the transcriptomic sequences. 8431-8442 (2015) This is the first study to characterize the leaf transcriptome of tree peony leaf using high-throughput sequencing. The information obtained from the tree peony leaf is valuable for gene discovery, and the identified heat shock protein genes can be used to improve plant stress-tolerance.

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ZmHSP16.9, a cytosolic class I small heat shock protein in maize (Zea mays), confers heat tolerance in transgenic tobacco

Abstract: The overexpression of ZmHSP16.9 enhanced tolerance to heat and oxidative stress in transgenic tobacco.

Cited by 115 publications

References 45 publications

Class I and II small heat-shock proteins protect protein translation factors during heat stress

Class I and II small heat-shock proteins protect protein translation factors during heat stress

Heat-resistant protein expression during germination of maize seeds under water stress

Identification of heat shock proteins via transcriptome profiling of tree peony leaf exposed to high temperature

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