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Relevant bibliographies by topics / HSP18.5

Academic literature on the topic 'HSP18.5'

Author: Grafiati

Published: 6 September 2023

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Journal articles on the topic "HSP18.5"

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Liu, Peng, Jundong Jia, Hanwen Wu, Zihan Song, and Xi He. "Hsp from Lactobacillus plantarum Expression in Lactococcus lactis MG1363." BIO Web of Conferences 61 (2023): 01010. http://dx.doi.org/10.1051/bioconf/20236101010.

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Small heat shock proteins are protective proteins produced by organisms under thermal stress. They are widely present in living organisms. Here, Hsp18, Hsp18.55 and Hsp19.5 genes were cloned from Lactobacillus plantarum and heterologous expressed in Lactococcus lactis, and their potential functions under ethanol stress were investigated. The results showed that the recombinant strain over expressing Hsp19.5 gene had stronger stress resistance, which provided a basis for further study of the survival ability of other microorganisms under ethanol stress.

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Kurre, Devanshu, and Kaza Suguna. "Network of Entamoeba histolytica HSP18.5 dimers formed by two overlapping [IV]‐X‐[IV] motifs." Proteins: Structure, Function, and Bioinformatics 89, no. 8 (April 8, 2021): 1039–54. http://dx.doi.org/10.1002/prot.26081.

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Kokke, Bas P. A., Michel R. Leroux, E. Peter M. Candido, Wilbert C. Boelens, and Wilfried W. de Jong. "Caenorhabditis eleganssmall heat-shock proteins Hsp12.2 and Hsp12.3 form tetramers and have no chaperone-like activity." FEBS Letters 433, no. 3 (August 21, 1998): 228–32. http://dx.doi.org/10.1016/s0014-5793(98)00917-x.

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Otani, Mieko, Toshiyuki Ueki, Satoshi Kozuka, Miki Segawa, Keiji Sano, and Sumiko Inouye. "Characterization of a Small Heat Shock Protein, Mx Hsp16.6, of Myxococcus xanthus." Journal of Bacteriology 187, no. 15 (August 1, 2005): 5236–41. http://dx.doi.org/10.1128/jb.187.15.5236-5241.2005.

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ABSTRACT A number of heat shock proteins in Myxococcus xanthus were previously identified by two-dimensional (2D) gel electrophoresis. One of these protein was termed Mx Hsp16.6, and the gene encoding Mx Hsp16.6 was isolated. Mx Hsp16.6 consists of 147 amino acid residues and has an estimated molecular weight of 16,642, in accordance with the apparent molecular mass in the 2D gel. An α-crystallin domain, typically conserved in small heat shock proteins, was found in Mx Hsp16.6. Mx Hsp16.6 was not detected during normal vegetative growth but was immediately induced after heat shock. Expression of the hsp16.6 gene was not induced by other stresses, such as starvation, oxidation, and high osmolarity. Mx Hsp16.6 was mostly localized in particles formed after heat shock and precipitated by low-speed centrifugation. Furthermore, Mx Hsp16.6 was detected in highly electron-dense particles in heat-shocked cells by immunoelectron microscopy, suggesting that it forms large complexes with heat-denatured proteins. An insertion mutation in the hsp16.6 gene resulted in lower viability during heat shock and lower acquired thermotolerance. Therefore, it is likely that Mx Hsp16.6 plays critical roles in the heat shock response in M. xanthus.

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Löw, Daniela, Kurt Brändle, Lutz Nover, and Christoph Forreiter. "Cytosolic heat-stress proteins Hsp17.7 class I and Hsp17.3 class II of tomato act as molecular chaperones in vivo." Planta 211, no. 4 (September 15, 2000): 575–82. http://dx.doi.org/10.1007/s004250000315.

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Zhang, Yanhao, Shanshan Li, Qianyi Liu, Ruiying Long, Jihong Feng, Huan Qin, Mao Li, Liping Liu, and Junmin Luo. "Mycobacterium tuberculosis Heat-Shock Protein 16.3 Induces Macrophage M2 Polarization Through CCRL2/CX3CR1." Inflammation 43, no. 2 (November 20, 2019): 487–506. http://dx.doi.org/10.1007/s10753-019-01132-9.

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Abstract Mycobacterium tuberculosis, the pathogen of tuberculosis (TB), can survive in host macrophages and induce macrophages to M2 phenotype might result in latent MTB infection. During the latent phase, the expression of MTB heat-shock protein 16.3 (Hsp16.3) is markedly increased among most of bacterial proteins, but the role of Hsp16.3 in macrophage M2 polarization is not clear. In this work, we found that macrophages incubated with 100 ng/ml MTB Hsp16.3 increased the production of Arg-1, IL-10, TGF-beta, and CD206. These results showed that MTB Hsp16.3 may induce macrophage M2 phenotype. And the interaction of Hsp16.3 with macrophages was found to depend on chemokine receptors CCRL2 and CX3CR1. Additionally, we used overexpression and silencing techniques to further verify the effect of CCRL2 and CX3CR1 on MTB Hsp16.3-induced M2 polarization macrophages. Furthermore, we explored the downstream signaling molecules of CCRL2 and CX3CR1 and we found MTB Hsp16.3 altered the signal transduction of the AKT/ERK/p38-MAPK. Taken together, this study provides evidence that MTB Hsp16.3 promotes macrophages to M2 phenotype and explores its underlying mechanism.

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Ma, Pengfei, Jie Li, Lei Qi, and Xiuzhu Dong. "The Archaeal Small Heat Shock Protein Hsp17.6 Protects Proteins from Oxidative Inactivation." International Journal of Molecular Sciences 22, no. 5 (March 4, 2021): 2591. http://dx.doi.org/10.3390/ijms22052591.

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Small heat shock proteins (sHsps) are widely distributed among various types of organisms and function in preventing the irreversible aggregation of thermal denaturing proteins. Here, we report that Hsp17.6 from Methanolobus psychrophilus exhibited protection of proteins from oxidation inactivation. The overexpression of Hsp17.6 in Escherichia coli markedly increased the stationary phase cell density and survivability in HClO and H2O2. Treatments with 0.2 mM HClO or 10 mM H2O2 reduced malate dehydrogenase (MDH) activity to 57% and 77%, whereas the addition of Hsp17.6 recovered the activity to 70–90% and 86–100%, respectively. A similar effect for superoxide dismutase oxidation was determined for Hsp17.6. Non-reducing sodium dodecyl sulfate polyacrylamide gel electrophoresis assays determined that the Hsp17.6 addition decreased H2O2-caused disulfide-linking protein contents and HClO-induced degradation of MDH; meanwhile, Hsp17.6 protein appeared to be oxidized with increased molecular weights. Mass spectrometry identified oxygen atoms introduced into the larger Hsp17.6 molecules, mainly at the aspartate and methionine residues. Substitution of some aspartate residues reduced Hsp17.6 in alleviating H2O2- and HClO-caused MDH inactivation and in enhancing the E. coli survivability in H2O2 and HClO, suggesting that the archaeal Hsp17.6 oxidation protection might depend on an “oxidant sink” effect, i.e., to consume the oxidants in environments via aspartate oxidation.

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Wagner, Daniela, Jens Schneider-Mergener, and Christoph Forreiter. "Analysis of Chaperone Function and Formation of Hetero-oligomeric Complexes of Hsp18.1 and Hsp17.7, Representing Two Different Cytoplasmic sHSP Classes in Pisum sativum." Journal of Plant Growth Regulation 24, no. 3 (September 2005): 226–37. http://dx.doi.org/10.1007/s00344-005-0020-3.

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Zhang, L., C. Lohmann, R. Prändl, and F. Schöffl. "Heat Stress-Dependent DNA Binding of Arabidopsis Heat Shock Transcription Factor HSF1 to Heat Shock Gene Promoters in Arabidopsis Suspension Culture Cells in vivo." Biological Chemistry 384, no. 6 (June 16, 2003): 959–63. http://dx.doi.org/10.1515/bc.2003.108.

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AbstractUsing UV laser cross-linking and immunoprecipitation we measured the in vivo binding of Arabidopsis heat shock transcription factor HSF1 to the promoters of target genes, Hsp18.2 and Hsp70. The amplification of promoter sequences, co-precipitated with HSF1-specific antibodies, indicated that HSF1 is not bound in the absence of heat stress. Binding to promoter sequences of target genes is rapidly induced by heat stress, continues throughout the heat treatment, and declines during subsequent recovery at room temperature. The molecular mechanisms underlying the differences between Hsp18.2 and Hsp70 in the kinetics of HSF1/promoter binding and corresponding mRNA expression profiles are discussed.

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WANG, Z., B. LAI, J. CAO, Z. LI, L. QU, A. CAO, and L. LAI. "Hierarchical Unfolding of Mj HSP16.5." Acta Physico-Chimica Sinica 24, no. 10 (October 2008): 1745–50. http://dx.doi.org/10.1016/s1872-1508(08)60070-4.

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Dissertations / Theses on the topic "HSP18.5"

1

Saxena, Anita. "Role of Hsp105 in CFTR Biogenesis." University of Toledo Health Science Campus / OhioLINK, 2010. http://rave.ohiolink.edu/etdc/view?acc_num=mco1279120195.

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Fang, Feng. "EXPRESSION OF HEAT SHOCK GENES HSP16.6 AND HTPG IN THE CYANOBACTERIUM, SYNECHOCYSTIS SP. PCC 6803." Miami University / OhioLINK, 2003. http://rave.ohiolink.edu/etdc/view?acc_num=miami1060835729.

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SERVANT, PASCALE. "La reponse au choc thermique chez streptomyces albus : etude des genes groe et caracterisation de la proteine hsp18." Paris 7, 1994. http://www.theses.fr/1994PA077303.

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Une elevation brutale de temperature provoque chez tous les etres vivants une augmentation de la synthese de quelques proteines dont certaines, les chaperons, ont un role essentiel dans la vie cellulaire. Les proteines groes et groel appartiennent a cette famille. Chez streptomyces albus deux genes groel (groel1 et groel2) ont ete caracterises. Le gene groel1 precede d'un gene groes code pour une proteine de 58 kda (hsp58) et le gene groel2 code pour une proteine de 56 kda (hsp56). Une proteine de 18 kda, cpn18, correspondant a la partie n-terminale de groel1 a ete egalement purifiee. Afin d'aborder le role physiologique des genes groel, une nouvelle technique d'interruption des genes chez streptomyces a ete mise au point. Un adn non replicatif est introduit par conjugaison d'e. Coli a streptomyces et s'integre par recombinaison homologue. Cette technique nous a permis de montrer que groel2 est indispensable a toute temperature. Le gene groel1 peut etre interrompu de 800 pb, la region du gene codant pour cpn18 semble etre indispensable. L'analyse du mutant groel1 n'a pas permis de determiner une fonction particuliere pour hsp58. En parallele du travail effectue sur groel, une proteine de petit poids moleculaire a ete caracterisee: hsp18. Cette proteine est fortement induite par le choc thermique et est homologue aux antigenes de 14 kda de mycobacterium tuberculosis et de 18 kda de m. Leprae. L'analyse de la transcription a permis de detecter un transcrit fortement induit a 40c, mais non visible a 30c et de cartographier le promoteur p18. La proteine hsp18 possede un role dans le resistance a haute temperature. Une autre partie du travail correspond a l'etude de la regulation de l'expression des genes groel chez s. Albus: ces genes sont soumis a une regulation post-transcriptionnelle. Cette regulation fait intervenir une courte region interne au gene. Des experiences recentes mettent en evidence une regulation traductionnelle: le site de fixation au ribosome et le codon d'initiation semblent pieges par une structure secondaire de l'arnm. Mots clefs: choc thermique, streptomyces albus, groel, hsp18, regulation post-transcriptionnelle

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Boehm, Christian Reiner. "Gene expression control for synthetic patterning of bacterial populations and plants." Thesis, University of Cambridge, 2017. https://www.repository.cam.ac.uk/handle/1810/267842.

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The development of shape in multicellular organisms has intrigued human minds for millenia. Empowered by modern genetic techniques, molecular biologists are now striving to not only dissect developmental processes, but to exploit their modularity for the design of custom living systems used in bioproduction, remediation, and regenerative medicine. Currently, our capacity to harness this potential is fundamentally limited by a lack of spatiotemporal control over gene expression in multicellular systems. While several synthetic genetic circuits for control of multicellular patterning have been reported, hierarchical induction of gene expression domains has received little attention from synthetic biologists, despite its fundamental role in biological self-organization. In this thesis, I introduce the first synthetic genetic system implementing population-based AND logic for programmed hierarchical patterning of bacterial populations of Escherichia coli, and address fundamental prerequisites for implementation of an analogous genetic circuit into the emergent multicellular plant model Marchantia polymorpha. In both model systems, I explore the use of bacteriophage T7 RNA polymerase as a gene expression engine to control synthetic patterning across populations of cells. In E. coli, I developed a ratiometric assay of bacteriophage T7 RNA polymerase activity, which I used to systematically characterize different intact and split enzyme variants. I utilized the best-performing variant to build a three-color patterning system responsive to two different homoserine lactones. I validated the AND gate-like behavior of this system both in cell suspension and in surface culture. Then, I used the synthetic circuit in a membrane-based spatial assay to demonstrate programmed hierarchical patterning of gene expression across bacterial populations. To prepare the adaption of bacteriophage T7 RNA polymerase-driven synthetic patterning from the prokaryote E. coli to the eukaryote M. polymorpha, I developed a toolbox of genetic elements for spatial gene expression control in the liverwort: I analyzed codon usage across the transcriptome of M. polymorpha, and used insights gained to design codon-optimized fluorescent reporters successfully expressed from its nuclear and chloroplast genomes. For targeting of bacteriophage T7 RNA polymerase to these cellular compartments, I functionally validated nuclear localization signals and chloroplast transit peptides. For spatiotemporal control of bacteriophage T7 RNA polymerase in M. polymorpha, I characterized spatially restricted and inducible promoters. For facilitated posttranscriptional processing of target transcripts, I functionally validated viral enhancer sequences in M. polymorpha. Taking advantage of this genetic toolbox, I introduced inducible nuclear-targeted bacteriophage T7 RNA polymerase into M. polymorpha. I showed implementation of the bacteriophage T7 RNA polymerase/PT7 expression system accompanied by hypermethylation of its target nuclear transgene. My observations suggest operation of efficient epigenetic gene silencing in M. polymorpha, and guide future efforts in chassis engineering of this multicellular plant model. Furthermore, my results encourage utilization of spatiotemporally controlled bacteriophage T7 RNA polymerase as a targeted silencing system for functional genomic studies and morphogenetic engineering in the liverwort. Taken together, the work presented enhances our capacity for spatiotemporal gene expression control in bacterial populations and plants, facilitating future efforts in synthetic morphogenesis for applications in synthetic biology and metabolic engineering.

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Shih, Chung-Cheng, and 施駿成. "Cloning, Expression, Purification and Chaperone-like Activity of a Small Heat-shock Protein, HSP16.1, from Caenorhabditis elegans." Thesis, 2004. http://ndltd.ncl.edu.tw/handle/17108316576923005625.

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碩士
國立臺灣大學
生化科學研究所
92
Small heat shock proteins (sHSPs) form a diverse family of proteins that are produced under various stresses in all organisms. It has been shown that they have chaperone-like activity, which can bind unfolded or misfolded proteins and maintain them in a folding-competent state. The common structural features of small heat shock proteins comprise an N-terminal domain and a C-terminal tail, which flank the evolutionarily conserved α-crystallin domain. However, α-crystallin, a major protein class of most animal eye lenses, was also found to possess chaperone-like activity similar to small heat shock proteins. Thus sHSPs and α-crystallin constitute a superfamily of related molecular chaperones with similar chaperone-like activity and aggregation property. In this thesis, we cloned, overexpressed, and characterized the chaperone-like activity of HSP16.1 from Caenorhabditis elegans. The cDNA sequence encoding HSP16.1 was amplified using reverse transcriptase/ polymerase chain reaction (RT-PCR) based on the two primers designed according to the nucleotide sequences obtained from the database of C. elegans. After overexpression, HSP16.1 was purified by two different size-exclusion chromatographies. The result from gel-filtration showed that the molecular mass of native HSP16.1 is about 670 kDa, which is different from that estimated from native gradient-gel electrophoresis and analytical ultracentrifugation. Although the midpoint temperature for protein aggregation of HSP16.1 is about 86℃, the secondary structure gradually changes when the temperature is over 50℃, accompanied by the decrease of chaperone-like activity. In contrast to α-crystallin from mammalian eye lenses, the oligomeric complexes and chaperone-like activity of HSP16.1 do not change after preheating treatment. These results suggested that HSP16.1 may be a thermostable protein with refolding potential, and its secondary structure is important to its chaperone-like activity. It is also of interest to find that the increase of calcium ion causes the decrease of chaperone-like activity of HSP16.1. Detailed mechanistic study of this effect is currently in progress.

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Book chapters on the topic "HSP18.5"

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Hatayama, Takumi. "Mammalian 105-kDa Heat-Shock Protein HSP105 and Its Biological Function." In Thermotherapy for Neoplasia, Inflammation, and Pain, 371–81. Tokyo: Springer Japan, 2001. http://dx.doi.org/10.1007/978-4-431-67035-3_42.

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Saito, Youhei, and Yuji Nakayama. "Mammalian Heat Shock Protein Hsp105: The Hsp70 Inducer and a Potent Target for Cancer Therapy." In HSP70 in Human Diseases and Disorders, 347–59. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-89551-2_18.

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Conference papers on the topic "HSP18.5"

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Pupa, Serenella M., Roberta Zappasodi, Italia Bongarzone, Antonello Cabras, Gaia C. Ghedini, Lorenzo Castagnoli, Francesca Micciché, Massimo A. Gianni, and Massimo Di Nicola. "Abstract 4785: Identification of HSP105 as a novel non-Hodgkin lymphoma (NHL) restricted antigen." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-4785.

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Reports on the topic "HSP18.5"

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Blum, Abraham, Henry T. Nguyen, and N. Y. Klueva. The Genetics of Heat Shock Proteins in Wheat in Relation to Heat Tolerance and Yield. United States Department of Agriculture, August 1993. http://dx.doi.org/10.32747/1993.7568105.bard.

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Fifty six diverse spring wheat cultivars were evaluated for genetic variation and heritability for thermotolerance in terms of cell-membrane stability (CMS) and triphenyl tetrazolium chloride (TTC) reduction. The most divergent cultivars for thermotolerance (Danbata-tolerant and Nacozari-susceptible) were crossed to develop an F8 random onbred line (RIL) population. This population was evaluated for co-segragation in CMS, yield under heat stress and HSP accumulation. Further studies of thermotolerance in relations to HSP and the expression of heterosis for growth under heat stress were performed with F1 hybrids of wheat and their parental cultivars. CMS in 95 RILs ranged from 76.5% to 22.4% with 71.5% and 31.3% in Danbata and Nacozari, respectively. The population segregated with a normal distribution across the full range of the parental values. Yield and biomass under non-stress conditions during the normal winter season at Bet Dagan dit not differ between the two parental cultivar, but the range of segregation for these traits in 138 RILs was very high and distinctly transgressive with a CV of 35.3% and 42.4% among lines for biomass and yield, respectively. Mean biomass and yield of the population was reduced about twofold when grown under the hot summer conditions (irrigated) at Bet Dagan. Segregation for biomass and yield was decreased relative to the normal winter conditions with CV of 20.2% and 23.3% among lines for biomass and yield, respectively. However, contrary to non-stress conditions, the parental cultivars differed about twofold in biomass and yield under heat stress and the population segregated with normal distribution across the full range of this difference. CMS was highly and positively correlated across 79 RILs with biomass (r=0.62**) and yield (r=0.58**) under heat stress. No such correlation was obtained under the normal winter conditions. All RILs expressed a set of HSPs under heat shock (37oC for 2 h). No variation was detected among RILs in high molecular weight HSP isoforms and they were similar to the patterns of the parental cultivars. There was a surprisingly low variability in low molecular weight HSP isoforms. Only one low molecular weight and Nacozari-specific HSP isoform (belonging to HSP 16.9 family) appeared to segregate among all RILs, but it was not quantitatively correlated with any parameter of plant production under heat stress or with CMS in this population. It is concluded that this Danbata/Nacozari F8 RIL population co-segregated well for thermotolerance and yield under heat stress and that CMS could predict the relative productivity of lines under chronic heat stress. Regretfully this population did not express meaningful variability for HSP accumulation under heat shock and therefore no role could be seen for HSP in the heat tolerance of this population. In the study of seven F1 hybrids and their parent cultivars it was found that heterosis (superiority of the F1 over the best parent) for CMs was generally lower than that for growth under heat stress. Hybrids varied in the rate of heterosis for growth at normal (15o/25o) and at high (25o/35o) temperatures. In certain hybrids heterosis for growth significantly increased at high temperature as compared with normal temperature, suggesting temperature-dependent heterosis. Generally, under normal temperature, only limited qualitative variation was detected in the patterns of protein synthesis in four wheat hybrids and their parents. However, a singular protein (C47/5.88) was specifically expressed only in the most heterotic hybrid at normal temperature but not in its parent cultivars. Parental cultivars were significantly different in the sets of synthesized HSP at 37o. No qualitative changes in the patterns of protein expression under heat stress were correlated with heterosis. However, a quantitative increase in certain low molecular weight HSP (mainly H14/5.5 and H14.5.6, belonging to the HSP16.9 family) was positively associated with greater heterosis for growth at high temperature. None of these proteins were correlated with CMS across hybrids. These results support the concept of temperature-dependent heterosis for growth and a possible role for HSP 16.9 family in this respect. Finally, when all experiments are viewed together, it is encouraging to find that genetic variation in wheat yield under chronic heat stress is associated with and well predicted by CMS as an assay of thermotolerance. On the other hand the results for HSP are elusive. While very low genetic variation was expressed for HSP in the RIL population, a unique low molecular weight HSP (of the HSP 16.9 family) could be associated with temperature dependant heterosis for growth.

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