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Artículos de revistas sobre el tema "HSFA2"

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Autor: Grafiati

Publicado: 4 de junio de 2021

Última modificación: 1 de febrero de 2022

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1

Scharf, Klaus-Dieter, Harald Heider, Ingo Höhfeld, Ruth Lyck, Enrico Schmidt y Lutz Nover. "The Tomato Hsf System: HsfA2 Needs Interaction with HsfA1 for Efficient Nuclear Import and May Be Localized in Cytoplasmic Heat Stress Granules". Molecular and Cellular Biology 18, n.º 4 (1 de abril de 1998): 2240–51. http://dx.doi.org/10.1128/mcb.18.4.2240.

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ABSTRACT In heat-stressed (HS) tomato (Lycopersicon peruvianum) cell cultures, the constitutively expressed HS transcription factor HsfA1 is complemented by two HS-inducible forms, HsfA2 and HsfB1. Because of its stability, HsfA2 accumulates to fairly high levels in the course of a prolonged HS and recovery regimen. Using immunofluorescence and cell fractionation experiments, we identified three states of HsfA2: (i) a soluble, cytoplasmic form in preinduced cultures maintained at 25°C, (ii) a salt-resistant, nuclear form found in HS cells, and (iii) a stored form of HsfA2 in cytoplasmic HS granules. The efficient nuclear transport of HsfA2 evidently requires interaction with HsfA1. When expressed in tobacco protoplasts by use of a transient-expression system, HsfA2 is mainly retained in the cytoplasm unless it is coexpressed with HsfA1. The essential parts for the interaction and nuclear cotransport of the two Hsfs are the homologous oligomerization domain (HR-A/B region of the A-type Hsfs) and functional nuclear localization signal motifs of both partners. Direct physical interaction of the two Hsfs with formation of relatively stabile hetero-oligomers was shown by a two-hybrid test inSaccharomyces cerevisiae as well as by coimmunoprecipitation using tomato and tobacco whole-cell lysates.

2

Heerklotz, Dirk, Pascal Döring, Frank Bonzelius, Sybille Winkelhaus y Lutz Nover. "The Balance of Nuclear Import and Export Determines the Intracellular Distribution and Function of Tomato Heat Stress Transcription Factor HsfA2". Molecular and Cellular Biology 21, n.º 5 (1 de marzo de 2001): 1759–68. http://dx.doi.org/10.1128/mcb.21.5.1759-1768.2001.

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ABSTRACT Tomato heat stress transcription factor HsfA2 is a shuttling protein with dominant cytoplasmic localization as a result of a nuclear import combined with an efficient export. Besides the nuclear localization signal (NLS) adjacent to the oligomerization domain, a C-terminal leucine-rich motif functions as a nuclear export signal (NES). Mutant forms of HsfA2 with a defective or an absent NES are nuclear proteins. The same is true for the wild-type HsfA2 if coexpressed with HsfA1 or in the presence of export inhibitor leptomycin B (LMB). Fusion of the NES domain of HsfA2 to HsfB1, which is a nuclear protein, caused export of the HsfB1-A2NES hybrid protein, and this effect was reversed by the addition of LMB. Due to the lack of background problems, Chinese hamster ovary (CHO) cells represent an excellent system for expression and functional analysis of tomato Hsfs. The results faithfully reflect the situation found in plant cells (tobacco protoplasts). The intriguing role of NLS and NES accessibility for the intracellular distribution of HsfA2 is underlined by the results of heat stress treatments of CHO cells (41°C). Despite the fact that nuclear import and export are not markedly affected, HsfA2 remains completely cytoplasmic at 41°C even in the presence of LMB. The temperature-dependent conformational transition of HsfA2 with shielding of the NLS evidently needs intramolecular interaction between the internal HR-A/B and the C-terminal HR-C regions. It is not observed with the HR oligomerization domain (HR-A/B region) deletion form of HsfA2 or in HsfA2-HsfA1 hetero-oligomers.

3

Ren, Shixiong, Kaibiao Ma, Zhaogeng Lu, Gang Chen, Jiawen Cui, Peixi Tong, Li Wang, Nianjun Teng y Biao Jin. "Transcriptomic and Metabolomic Analysis of the Heat-Stress Response of Populus tomentosa Carr." Forests 10, n.º 5 (30 de abril de 2019): 383. http://dx.doi.org/10.3390/f10050383.

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Plants have evolved mechanisms of stress tolerance responses to heat stress. However, little is known about metabolic responses to heat stress in trees. In this study, we exposed Populus tomentosa Carr. to control (25 °C) and heat stress (45 °C) treatments and analyzed the metabolic and transcriptomic effects. Heat stress increased the cellular concentration of H2O2 and the activities of antioxidant enzymes. The levels of proline, raffinose, and melibiose were increased by heat stress, whereas those of pyruvate, fumarate, and myo-inositol were decreased. The expression levels of most genes (PSB27, PSB28, LHCA5, PETB, and PETC) related to the light-harvesting complexes and photosynthetic electron transport system were downregulated by heat stress. Association analysis between key genes and altered metabolites indicated that glycolysis was enhanced, whereas the tricarboxylic acid (TCA) cycle was suppressed. The inositol phosphate; galactose; valine, leucine, and isoleucine; and arginine and proline metabolic pathways were significantly affected by heat stress. In addition, several transcription factors, including HSFA2, HSFA3, HSFA9, HSF4, MYB27, MYB4R1, and bZIP60 were upregulated, whereas WRKY13 and WRKY50 were downregulated by heat stress. Interestingly, under heat stress, the expression of DREB1, DREB2, DREB2E, and DREB5 was dramatically upregulated at 12 h. Our results suggest that proline, raffinose, melibiose, and several genes (e.g., PSB27, LHCA5, and PETB) and transcription factors (e.g., HSFAs and DREBs) are involved in the response to heat stress in P. tomentosa.

4

Zupanska, Agata, Collin LeFrois, Robert Ferl y Anna-Lisa Paul. "HSFA2 Functions in the Physiological Adaptation of Undifferentiated Plant Cells to Spaceflight". International Journal of Molecular Sciences 20, n.º 2 (17 de enero de 2019): 390. http://dx.doi.org/10.3390/ijms20020390.

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Heat Shock Factor A2 (HsfA2) is part of the Heat Shock Factor (HSF) network, and plays an essential role beyond heat shock in environmental stress responses and cellular homeostatic control. Arabidopsis thaliana cell cultures derived from wild type (WT) ecotype Col-0 and a knockout line deficient in the gene encoding HSFA2 (HSFA2 KO) were grown aboard the International Space Station (ISS) to ascertain whether the HSF network functions in the adaptation to the novel environment of spaceflight. Microarray gene expression data were analyzed using a two-part comparative approach. First, genes differentially expressed between the two environments (spaceflight to ground) were identified within the same genotype, which represented physiological adaptation to spaceflight. Second, gene expression profiles were compared between the two genotypes (HSFA2 KO to WT) within the same environment, which defined genes uniquely required by each genotype on the ground and in spaceflight-adapted states. Results showed that the endoplasmic reticulum (ER) stress and unfolded protein response (UPR) define the HSFA2 KO cells’ physiological state irrespective of the environment, and likely resulted from a deficiency in the chaperone-mediated protein folding machinery in the mutant. Results further suggested that additional to its universal stress response role, HsfA2 also has specific roles in the physiological adaptation to spaceflight through cell wall remodeling, signal perception and transduction, and starch biosynthesis. Disabling HsfA2 altered the physiological state of the cells, and impacted the mechanisms induced to adapt to spaceflight, and identified HsfA2-dependent genes that are important to the adaption of wild type cells to spaceflight. Collectively these data indicate a non-thermal role for the HSF network in spaceflight adaptation.

5

Oh, Hye-Sook, Ora Son, Jong-Yoon Chun, Gary Stacey, Myung-Sok Lee, Kyung-Hee Min, Eun-Sook Song y Choong-III Cheon. "The Bradyrhizobium japonicum hsfA Gene Exhibits a Unique Developmental Expression Pattern in Cowpea Nodules". Molecular Plant-Microbe Interactions® 14, n.º 11 (noviembre de 2001): 1286–92. http://dx.doi.org/10.1094/mpmi.2001.14.11.1286.

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The Bradyrhizobium japonicum host-specific fixation gene hsfA was identified as essential for nitrogen fixation on cowpea, but not required for nitrogen fixation on soybean or siratro. The DNA sequence of the hsfA promoter contains a consensus RpoN, -24/-12 binding site, suggesting the involvement of a regulatory protein that binds to an upstream activating sequence (UAS). To further explore the regulation of this interesting gene, serial deletions of the hsfA promoter were made and fused with the β-glucuronidase (GUS) gene. The HsfA3 deletion, containing 60 bp 5′ of the -24/-12 sequence, showed a similar level of GUS expression to that shown by the longest fusion construct (HsfA1), containing 464 bp of upstream sequence. In contrast, the HsfA4-GUS fusion, containing only 20 bp 5′ of the -24/-12 region, showed no GUS activity, delimiting the location of a putative UAS to a 40-bp region. During nodule development, GUS expression first appeared in nodules 12 days postinoculation (dpi) and reached a maximum level of expression in approximately 17-day-old nodules. By 28 dpi, HsfA-GUS expression had returned to a low, basal level. These data were consistent with the detection of hsfA mRNA by in situ hybridization in 17-day-old nodules, but not in 28-day-old nodules. In contrast to the stage-specific expression in cowpea, HsfA-GUS expression increased with nodule development in HsfA3-inoculated soybean. These data indicate that HsfA expression is regulated in cowpea in a unique developmental manner and that the DNA regulatory regions that control this expression are confined to a short, promoter-proximal region.

6

Jacob, Pierre, Gwilherm Brisou, Marion Dalmais, Johanne Thévenin, Froukje van der Wal, David Latrasse, Ravi Suresh Devani et al. "The Seed Development Factors TT2 and MYB5 Regulate Heat Stress Response in Arabidopsis". Genes 12, n.º 5 (15 de mayo de 2021): 746. http://dx.doi.org/10.3390/genes12050746.

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HEAT SHOCK FACTOR A2 (HSFA2) is a regulator of multiple environmental stress responses required for stress acclimation. We analyzed HSFA2 co-regulated genes and identified 43 genes strongly co-regulated with HSFA2 during multiple stresses. Motif enrichment analysis revealed an over-representation of the site II element (SIIE) in the promoters of these genes. In a yeast 1-hybrid screen with the SIIE, we identified the closely related R2R3-MYB transcription factors TT2 and MYB5. We found overexpression of MYB5 or TT2 rendered plants heat stress tolerant. In contrast, tt2, myb5, and tt2/myb5 loss of function mutants showed heat stress hypersensitivity. Transient expression assays confirmed that MYB5 and TT2 can regulate the HSFA2 promoter together with the other members of the MBW complex, TT8 and TRANSPARENT TESTA GLABRA 1 (TTG1) and that the SIIE was involved in this regulation. Transcriptomic analysis revealed that TT2/MYB5 target promoters were enriched in SIIE. Overall, we report a new function of TT2 and MYB5 in stress resistance and a role in SIIE-mediated HSFA2 regulation.

7

Enomoto, Takuo, Mutsutomo Tokizawa, Hiroki Ito, Satoshi Iuchi, Masatomo Kobayashi, Yoshiharu Y. Yamamoto, Yuriko Kobayashi y Hiroyuki Koyama. "STOP1 regulates the expression of HsfA2 and GDHs that are critical for low-oxygen tolerance in Arabidopsis". Journal of Experimental Botany 70, n.º 12 (18 de marzo de 2019): 3297–311. http://dx.doi.org/10.1093/jxb/erz124.

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Abstract The SENSITIVE TO PROTON RHIZOTOXICITY 1 (STOP1) transcription factor regulates gene expression associated with multiple stress tolerances in plant roots. In this study, we investigated the mechanism responsible for the sensitivity of the stop1 mutant to low-oxygen stress in Arabidopsis. Transcriptomic analyses revealed that two genes involved in low-oxygen tolerance, namely GLUTAMATE DEHYDROGENASE 1 (GDH1) and GDH2, showed lower expression levels in the stop1 mutant than in the wild-type. Sensitivity of the gdh1gdh2 double-mutant to low-oxygen conditions was partly attributable to the low-oxygen sensitivity of the stop1 mutant. Two transcription factors, STOP2 and HEAT SHOCK FACTOR A2 (HsfA2), were expressed at lower levels in the stop1 mutant. An in planta complementation assay indicated that CaMV35S::STOP2 or CaMV35S::HsfA2 partially rescued the low-oxygen tolerance of the stop1 mutant, which was concomitant with recovered expression of genes regulating low-pH tolerance and genes encoding molecular chaperones. Prediction of cis-elements and in planta promoter assays revealed that STOP1 directly activated the expression of HsfA2. Similar STOP1-dependent low-oxygen sensitivity was detected in tobacco. Suppression of NtSTOP1 induced low-oxygen sensitivity, which was associated with lower expression levels of NtHsfA2 and NtGDHs compared with the wild-type. Our results indicated that STOP1 pleiotropically regulates low-oxygen tolerance by transcriptional regulation.

8

Singh, Garima, Neelam K. Sarkar y Anil Grover. "Tango between Ethylene and HSFA2 Settles Heat Tolerance". Trends in Plant Science 26, n.º 5 (mayo de 2021): 429–32. http://dx.doi.org/10.1016/j.tplants.2021.03.003.

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9

Doring, Pascal, Eckardt Treuter, Catherine Kistner, Ruth Lyck, Alexander Chen y Lutz Nover. "The Role of AHA Motifs in the Activator Function of Tomato Heat Stress Transcription Factors HsfA1 and HsfA2". Plant Cell 12, n.º 2 (febrero de 2000): 265. http://dx.doi.org/10.2307/3870927.

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10

Döring, Pascal, Eckardt Treuter, Catherine Kistner, Ruth Lyck, Alexander Chen y Lutz Nover. "The Role of AHA Motifs in the Activator Function of Tomato Heat Stress Transcription Factors HsfA1 and HsfA2". Plant Cell 12, n.º 2 (febrero de 2000): 265–78. http://dx.doi.org/10.1105/tpc.12.2.265.

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11

Lämke, Jörn, Krzysztof Brzezinka y Isabel Bäurle. "HSFA2 orchestrates transcriptional dynamics after heat stress inArabidopsis thaliana". Transcription 7, n.º 4 (6 de julio de 2016): 111–14. http://dx.doi.org/10.1080/21541264.2016.1187550.

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12

Xin, Haibo, Hua Zhang, Li Chen, Xiaoxin Li, Qinglong Lian, Xue Yuan, Xiaoyan Hu, Li Cao, Xiuli He y Mingfang Yi. "Cloning and characterization of HsfA2 from Lily (Lilium longiflorum)". Plant Cell Reports 29, n.º 8 (25 de mayo de 2010): 875–85. http://dx.doi.org/10.1007/s00299-010-0873-1.

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13

Chan-Schaminet, Kwan Yu, Sanjeev K. Baniwal, Daniela Bublak, Lutz Nover y Klaus-Dieter Scharf. "Specific Interaction between Tomato HsfA1 and HsfA2 Creates Hetero-oligomeric Superactivator Complexes for Synergistic Activation of Heat Stress Gene Expression". Journal of Biological Chemistry 284, n.º 31 (1 de junio de 2009): 20848–57. http://dx.doi.org/10.1074/jbc.m109.007336.

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14

Werghi, Sirine, Charfeddine Gharsallah, Nishi Kant Bhardwaj, Hatem Fakhfakh y Faten Gorsane. "Insights into the heat-responsive transcriptional network of tomato contrasting genotypes". Plant Genetic Resources: Characterization and Utilization 19, n.º 1 (febrero de 2021): 44–57. http://dx.doi.org/10.1017/s1479262121000083.

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AbstractDuring recent decades, global warming has intensified, altering crop growth, development and survival. To overcome changes in their environment, plants undergo transcriptional reprogramming to activate stress response strategies/pathways. To evaluate the genetic bases of the response to heat stress, Conserved DNA-derived Polymorphism (CDDP) markers were applied across tomato genome of eight cultivars. Despite scattered genotypes, cluster analysis allowed two neighbouring panels to be discriminate. Tomato CDDP-genotypic and visual phenotypic assortment permitted the selection of two contrasting heat-tolerant and heat-sensitive cultivars. Further analysis explored differential expression in transcript levels of genes, encoding heat shock transcription factors (HSFs, HsfA1, HsfA2, HsfB1), members of the heat shock protein (HSP) family (HSP101, HSP17, HSP90) and ascorbate peroxidase (APX) enzymes (APX1, APX2). Based on discriminating CDDP-markers, a protein functional network was built allowing prediction of candidate genes and their regulating miRNA. Expression patterns analysis revealed that miR156d and miR397 were heat-responsive showing a typical inverse relation with the abundance of their target gene transcripts. Heat stress is inducing a set of candidate genes, whose expression seems to be modulated through a complex regulatory network. Integrating genetic resource data is required for identifying valuable tomato genotypes that can be considered in marker-assisted breeding programmes to improve tomato heat tolerance.

15

Banti, Valeria, Fabrizio Mafessoni, Elena Loreti, Amedeo Alpi y Pierdomenico Perata. "The Heat-Inducible Transcription Factor HsfA2 Enhances Anoxia Tolerance in Arabidopsis". Plant Physiology 152, n.º 3 (20 de enero de 2010): 1471–83. http://dx.doi.org/10.1104/pp.109.149815.

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16

Liu, Junzhong, Lili Feng, Xueting Gu, Xian Deng, Qi Qiu, Qun Li, Yingying Zhang et al. "An H3K27me3 demethylase-HSFA2 regulatory loop orchestrates transgenerational thermomemory in Arabidopsis". Cell Research 29, n.º 5 (18 de febrero de 2019): 379–90. http://dx.doi.org/10.1038/s41422-019-0145-8.

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17

NISHIZAWA-YOKOI, Ayako, Eriko YOSHIDA, Yukinori YABUTA y Shigeru SHIGEOKA. "Analysis of the Regulation of Target Genes by anArabidopsisHeat Shock Transcription Factor, HsfA2". Bioscience, Biotechnology, and Biochemistry 73, n.º 4 (23 de abril de 2009): 890–95. http://dx.doi.org/10.1271/bbb.80809.

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18

Kataoka, Ryo, Misato Takahashi y Nobuhiro Suzuki. "Coordination between bZIP28 and HSFA2 in the regulation of heat response signals in Arabidopsis". Plant Signaling & Behavior 12, n.º 11 (20 de octubre de 2017): e1376159. http://dx.doi.org/10.1080/15592324.2017.1376159.

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19

Liu, Jinjie, Na Sun, Meng Liu, Jiancheng Liu, Bojing Du, Xinjing Wang y Xiaoting Qi. "An Autoregulatory Loop Controlling Arabidopsis HsfA2 Expression: Role of Heat Shock-Induced Alternative Splicing". Plant Physiology 162, n.º 1 (15 de marzo de 2013): 512–21. http://dx.doi.org/10.1104/pp.112.205864.

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20

Cohen-Peer, Reut, Silvia Schuster, David Meiri, Adina Breiman y Adi Avni. "Sumoylation of Arabidopsis heat shock factor A2 (HsfA2) modifies its activity during acquired thermotholerance". Plant Molecular Biology 74, n.º 1-2 (4 de junio de 2010): 33–45. http://dx.doi.org/10.1007/s11103-010-9652-1.

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21

Heerklotz, Dirk, Raffaella Calligaris, Sybille Winkelhaus, Marc Kirschner, Lutz Nover y Klaus-Dieter Scharf. "NUCLEAR EXPORT AND INTERACTION WITH CYTOPLASMIC CHAPERONE COMPLEXES OF TOMATO HEAT STRESS TRANSCRIPTION FACTOR HSFA2". Biochemical Society Transactions 28, n.º 5 (1 de octubre de 2000): A351. http://dx.doi.org/10.1042/bst028a351a.

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22

Charng, Yee-yung, Hsiang-chin Liu, Nai-yu Liu, Wen-tzu Chi, Chun-neng Wang, Shih-hsun Chang y Tsu-tsuen Wang. "A Heat-Inducible Transcription Factor, HsfA2, Is Required for Extension of Acquired Thermotolerance in Arabidopsis". Plant Physiology 143, n.º 1 (3 de noviembre de 2006): 251–62. http://dx.doi.org/10.1104/pp.106.091322.

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23

Evrard, Alexandre, Mukesh Kumar, David Lecourieux, Jessica Lucks, Pascal von Koskull-Döring y Heribert Hirt. "Regulation of the heat stress response inArabidopsisby MPK6-targeted phosphorylation of the heat stress factor HsfA2". PeerJ 1 (2 de abril de 2013): e59. http://dx.doi.org/10.7717/peerj.59.

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24

Giorno, Filomena, Mieke Wolters-Arts, Stefania Grillo, Klaus-Dieter Scharf, Wim H. Vriezen y Celestina Mariani. "Developmental and heat stress-regulated expression of HsfA2 and small heat shock proteins in tomato anthers". Journal of Experimental Botany 61, n.º 2 (23 de octubre de 2009): 453–62. http://dx.doi.org/10.1093/jxb/erp316.

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25

Hu, Yangjie, Anida Mesihovic, José M. Jiménez‐Gómez, Sascha Röth, Philipp Gebhardt, Daniela Bublak, Arnaud Bovy, Klaus‐Dieter Scharf, Enrico Schleiff y Sotirios Fragkostefanakis. "Natural variation in HsfA2 pre‐mRNA splicing is associated with changes in thermotolerance during tomato domestication". New Phytologist 225, n.º 3 (14 de noviembre de 2019): 1297–310. http://dx.doi.org/10.1111/nph.16221.

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26

Port, Markus, Joanna Tripp, Dirk Zielinski, Christian Weber, Dirk Heerklotz, Sybille Winkelhaus, Daniela Bublak y Klaus-Dieter Scharf. "Role of Hsp17.4-CII as Coregulator and Cytoplasmic Retention Factor of Tomato Heat Stress Transcription Factor HsfA2". Plant Physiology 135, n.º 3 (julio de 2004): 1457–70. http://dx.doi.org/10.1104/pp.104.042820.

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27

Meiri, David y Adina Breiman. "Arabidopsis ROF1 (FKBP62) modulates thermotolerance by interacting with HSP90.1 and affecting the accumulation of HsfA2-regulated sHSPs". Plant Journal 59, n.º 3 (agosto de 2009): 387–99. http://dx.doi.org/10.1111/j.1365-313x.2009.03878.x.

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28

Yu, Hai-Dong, Xiao-Fei Yang, Si-Ting Chen, Yu-Ting Wang, Ji-Kai Li, Qi Shen, Xun-Liang Liu y Fang-Qing Guo. "Downregulation of Chloroplast RPS1 Negatively Modulates Nuclear Heat-Responsive Expression of HsfA2 and Its Target Genes in Arabidopsis". PLoS Genetics 8, n.º 5 (3 de mayo de 2012): e1002669. http://dx.doi.org/10.1371/journal.pgen.1002669.

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29

Fragkostefanakis, Sotirios, Anida Mesihovic, Stefan Simm, Marine Josephine Paupière, Yangjie Hu, Puneet Paul, Shravan Kumar Mishra et al. "HsfA2 Controls the Activity of Developmentally and Stress-Regulated Heat Stress Protection Mechanisms in Tomato Male Reproductive Tissues". Plant Physiology 170, n.º 4 (25 de febrero de 2016): 2461–77. http://dx.doi.org/10.1104/pp.15.01913.

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30

Piveta, Leonard Bonilha, Nilda Roma-Burgos, José Alberto Noldin, Vívian Ebeling Viana, Claudia de Oliveira, Fabiane Pinto Lamego y Luis Antonio de Avila. "Molecular and Physiological Responses of Rice and Weedy Rice to Heat and Drought Stress". Agriculture 11, n.º 1 (24 de diciembre de 2020): 9. http://dx.doi.org/10.3390/agriculture11010009.

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Rice is the staple food for about half of the world population. Rice grain yield and quality are affected by climatic changes. Arguably, rice cultivars’ genetic diversity is diminished from decades of breeding using narrow germplasm, requiring introgressions from other Oryza species, weedy or wild. Weedy rice has high genetic diversity, which is an essential resource for rice crop improvement. Here, we analyzed the phenotypic, physiological, and molecular profiles of two rice cultivars (IRGA 424 and SCS119 Rubi) and five weedy rice (WR), from five different Brazilian regions, in response to heat and drought stress. Drought and heat stress affected the phenotype and photosynthetic parameters in different ways in rice and WR genotypes. A WR from Northern Brazil yielded better under heat stress than the non-stressed check. Drought stress upregulated HSF7A while heat stress upregulated HSF2a. HSP74.8, HSP80.2, and HSP24.1 were upregulated in both conditions. Based on all evaluated traits, we hypothesized that in drought conditions increasing HSFA7 expression is related to tiller number and that increase WUE (water use efficiency) and HSFA2a expression are associated with yield. In heat conditions, Gs (stomatal conductance) and E’s increases may be related to plant height; tiller number is inversely associated with HSPs expression, and chlorophyll content and Ci (intercellular CO2 concentration) may be related to yield. Based on morphology, physiology, and gene regulation in heat and drought stress, we can discriminate genotypes that perform well under these stress conditions and utilize such genotypes as a source of genetic diversity for rice breeding.

31

Nishizawa-Yokoi, Ayako, Hitoshi Tainaka, Eriko Yoshida, Masahiro Tamoi, Yukinori Yabuta y Shigeru Shigeoka. "The 26S Proteasome Function and Hsp90 Activity Involved in the Regulation of HsfA2 Expression in Response to Oxidative Stress". Plant and Cell Physiology 51, n.º 3 (9 de enero de 2010): 486–96. http://dx.doi.org/10.1093/pcp/pcq015.

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32

Masuda, Shinji, Yoshihito Tokaji, Yuichi Kobayashi y Hiroyuki Ohta. "Mechanisms of induction of the stress-responsive transcription factors HsfA2 and DREB2A by 12-oxo-phytodienoic acid inArabidopsis thaliana". Bioscience, Biotechnology, and Biochemistry 78, n.º 4 (3 de abril de 2014): 647–50. http://dx.doi.org/10.1080/09168451.2014.891929.

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33

Baniwal, Sanjeev K., Kwan Yu Chan, Klaus-Dieter Scharf y Lutz Nover. "Role of Heat Stress Transcription Factor HsfA5 as Specific Repressor of HsfA4". Journal of Biological Chemistry 282, n.º 6 (febrero de 2007): 3605–13. http://dx.doi.org/10.1074/jbc.m609545200.

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34

Zhang, Lingrui, Yinshu Li, Da Xing y Caiji Gao. "Characterization of mitochondrial dynamics and subcellular localization of ROS reveal that HsfA2 alleviates oxidative damage caused by heat stress in Arabidopsis". Journal of Experimental Botany 60, n.º 7 (2 de abril de 2009): 2073–91. http://dx.doi.org/10.1093/jxb/erp078.

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35

Arofatullah, Nur Akbar, Morifumi Hasegawa, Sayuri Tanabata, Isao Ogiwara y Tatsuo Sato. "Heat Shock-Induced Resistance Against Pseudomonas syringae pv. tomato (Okabe) Young et al. via Heat Shock Transcription Factors in Tomato". Agronomy 9, n.º 1 (20 de diciembre de 2018): 2. http://dx.doi.org/10.3390/agronomy9010002.

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*Abstract: We investigated the role of heat shock transcription factors (Hsfs) during induction of defense response by heat-shock treatment (HST) in tomato. Leaf disease symptoms were significantly reduced at 12 and 24 h after HST, consistent with upregulation of pathogenesis-related (PR) genes PR1a2 and PR1b1 peaking at 24 h after treatment. These genes were upregulated at the treatment application site, but not in untreated leaves. In contrast to HST, inoculation of the first leaf induced systemic upregulation of acidic PR genes in uninoculated second leaves. Furthermore, heat shock element motifs were found in upstream regions of PR1a2, PR1b1, Chitinase 3, Chitinase 9, Glucanase A, and Glucanase B genes. Upregulation of HsfA2 and HsfB1 peaked at 6 h after HST, 6 h earlier than salicylic acid accumulation. Foliar spray of heat shock protein 90 (Hsp90) inhibitor geldanamycin (GDA) induced PR gene expression comparable to that after HST. PR gene expression and defense response against Pseudomonas syringae pv. tomato (Pst) decreased when combining HST with Hsfs inhibitor KRIBB11. The Hsfs and PR gene expression induced by heat or GDA, together with the suppression of heat shock-induced resistance (HSIR) against Pst by KRIBB11, suggested a direct contribution of Hsfs to HSIR regulation in tomato.

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Maleckova, Eva, Dominik Brilhaus, Thomas J. Wrobel y Andreas P. M. Weber. "Transcript and metabolite changes during the early phase of abscisic acid-mediated induction of crassulacean acid metabolism in Talinum triangulare". Journal of Experimental Botany 70, n.º 22 (24 de abril de 2019): 6581–96. http://dx.doi.org/10.1093/jxb/erz189.

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Abstract Crassulacean acid metabolism (CAM) has evolved as a water-saving strategy, and its engineering into crops offers an opportunity to improve their water use efficiency. This requires a comprehensive understanding of the regulation of the CAM pathway. Here, we use the facultative CAM species Talinum triangulare as a model in which CAM can be induced rapidly by exogenous abscisic acid. RNA sequencing and metabolite measurements were employed to analyse the changes underlying CAM induction and identify potential CAM regulators. Non-negative matrix factorization followed by k-means clustering identified an early CAM-specific cluster and a late one, which was specific for the early light phase. Enrichment analysis revealed abscisic acid metabolism, WRKY-regulated transcription, sugar and nutrient transport, and protein degradation in these clusters. Activation of the CAM pathway was supported by up-regulation of phosphoenolpyruvate carboxylase, cytosolic and chloroplastic malic enzymes, and several transport proteins, as well as by increased end-of-night titratable acidity and malate accumulation. The transcription factors HSFA2, NF-YA9, and JMJ27 were identified as candidate regulators of CAM induction. With this study we promote the model species T. triangulare, in which CAM can be induced in a controlled way, enabling further deciphering of CAM regulation.

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Ogawa, D., K. Yamaguchi y T. Nishiuchi. "High-level overexpression of the Arabidopsis HsfA2 gene confers not only increased themotolerance but also salt/osmotic stress tolerance and enhanced callus growth". Journal of Experimental Botany 58, n.º 12 (13 de julio de 2007): 3373–83. http://dx.doi.org/10.1093/jxb/erm184.

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Schramm, Franziska, Arnab Ganguli, Elke Kiehlmann, Gisela Englich, Daniela Walch y Pascal von Koskull-Döring. "The Heat Stress Transcription Factor HsfA2 Serves as a Regulatory Amplifier of a Subset of Genes in the Heat Stress Response in Arabidopsis". Plant Molecular Biology 60, n.º 5 (marzo de 2006): 759–72. http://dx.doi.org/10.1007/s11103-005-5750-x.

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Nishizawa-Yokoi, Ayako, Ryota Nosaka, Hideki Hayashi, Hitoshi Tainaka, Takanori Maruta, Masahiro Tamoi, Miho Ikeda et al. "HsfA1d and HsfA1e Involved in the Transcriptional Regulation of HsfA2 Function as Key Regulators for the Hsf Signaling Network in Response to Environmental Stress". Plant and Cell Physiology 52, n.º 5 (6 de abril de 2011): 933–45. http://dx.doi.org/10.1093/pcp/pcr045.

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Chen, Xuan, Xiulian Yang, Jun Xie, Wenjie Ding, Yuli Li, Yuanzheng Yue y Lianggui Wang. "Biochemical and Comparative Transcriptome Analyses Reveal Key Genes Involved in Major Metabolic Regulation Related to Colored Leaf Formation in Osmanthus fragrans ‘Yinbi Shuanghui’ during Development". Biomolecules 10, n.º 4 (4 de abril de 2020): 549. http://dx.doi.org/10.3390/biom10040549.

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Osmanthus fragrans ‘Yinbi Shuanghui’ not only has a beautiful shape and fresh floral fragrance, but also rich leaf colors that change, making the tree useful for landscaping. In order to study the mechanisms of color formation in O. fragrans ‘Yinbi Shuanghui’ leaves, we analyzed the colored and green leaves at different developmental stages in terms of leaf pigment content, cell structure, and transcriptome data. We found that the chlorophyll content in the colored leaves was lower than that of green leaves throughout development. By analyzing the structure of chloroplasts, the colored leaves demonstrated more stromal lamellae and low numbers of granum thylakoid. However, there was a large number of plastoglobuli. Using transcriptome sequencing, we demonstrated that the expression of differentially expressed genes (DEGs) involved in chlorophyll degradation was upregulated, i.e., heme oxygennase-1 (HO1), pheophorbide a oxidase (PAO), and chlorophyllase-2 (CLH2), affecting the synthesis of chlorophyll in colored leaves. The stay-green gene (SGR) was upregulated in colored leaves. Genes involved in carotenoid synthesis, i.e., phytoene synthase 1 (PSY1) and 1-Deoxyxylulose-5-phosphate synthase (DXS), were downregulated in colored leaves, impeding the synthesis of carotenoids. In the later stage of leaf development, the downregulated expression of Golden2-Like (GLK) inhibited chloroplast development in colored leaves. Using weighted gene co-expression network analysis (WGCNA) to investigate the correlation between physiological indicators and DEGs, we chose the modules with the highest degree of relevance to chlorophyll degradation and carotenoid metabolism. A total of five genes (HSFA2, NFYC9, TCP20, WRKY3, and WRKY4) were identified as hub genes. These analyses provide new insights into color formation mechanisms in O. fragrans ‘Yinbi Shuanghui’ leaves at the transcriptional level.

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Sojka, Damian Robert, Agnieszka Gogler-Pigłowska, Katarzyna Klarzyńska, Marta Klimczak, Alicja Zylicz, Magdalena Głowala-Kosińska, Zdzisław Krawczyk y Dorota Scieglinska. "HSPA2 Chaperone Contributes to the Maintenance of Epithelial Phenotype of Human Bronchial Epithelial Cells but Has Non-Essential Role in Supporting Malignant Features of Non-Small Cell Lung Carcinoma, MCF7, and HeLa Cancer Cells". Cancers 12, n.º 10 (24 de septiembre de 2020): 2749. http://dx.doi.org/10.3390/cancers12102749.

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Heat Shock Protein A2 (HSPA2) is a member of the HSPA (HSP70) chaperone family and has a critical role for male fertility. HSPA2 is present in a number of somatic organs. Limited evidence suggests that HSPA2 may be involved in regulating epithelial cell differentiation. HSPA2 also emerged as a cancer-related chaperone; however, no consensus on its functional significance has been reached so far. In this study, we compared the phenotypic effects of HSPA2 deficit in non-transformed human bronchial epithelial cells (HBEC), and in lung, breast, and cervical cancer cells. We used various techniques to inhibit the HSPA2 gene expression in order to examine the impact of HSPA2 deficiency on cell growth, migration, adhesion, and invasion. Our results show that HBEC but not cancer cells are sensitive to HSPA2 deficit. HSPA2 knockdown in HBEC cells impaired their clone-forming ability and adhesiveness. Thus, our results indicate that epithelial cells can rely on a specific activity of HSPA2, but such dependence can be lost in epithelial cells that have undergone malignant transformation.

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Filipczak, Piotr Teodor, Wojciech Piglowski, Magdalena Glowala-Kosinska, Zdzislaw Krawczyk y Dorota Scieglinska. "HSPA2 overexpression protects V79 fibroblasts against bortezomib-induced apoptosis". Biochemistry and Cell Biology 90, n.º 2 (abril de 2012): 224–31. http://dx.doi.org/10.1139/o11-083.

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Human HSPA2 is a member of the HSPA (HSP70) family of heat-shock proteins, encoded by the gene originally described as testis-specific. Recently, it has been reported that HSPA2 can be also expressed in human somatic tissues in a cell-type specific manner. The aim of the present study was to find out whether HSPA2 can increase the resistance of somatic cells to the toxic effect of heat shock, proteasome inhibitors, and several anticancer cytostatics. We used a Chinese hamster fibroblast V79 cell line because these cells do not express the HSPA2 and cytoprotective HSPA1 proteins under normal culture conditions and show limited ability to express HSPA1 in response to heat shock and proteasome inhibitors. We established, by retroviral gene transfer, a stable V79/HSPA2 cell line, which constitutively overexpressed HSPA2 protein. The major observation of our study was that HSPA2 increased long-term survival of cells subjected to heat shock and proteasome inhibitors. We found, that HSPA2 confers resistance to bortezomib-induced apoptosis. Thus, we showed for the first time that in somatic cells HSPA2 can be a part of a system protecting cells against cytotoxic stimuli inducing proteotoxic stress.

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Goodson, M. L., O. K. Park-Sarge y K. D. Sarge. "Tissue-dependent expression of heat shock factor 2 isoforms with distinct transcriptional activities." Molecular and Cellular Biology 15, n.º 10 (octubre de 1995): 5288–93. http://dx.doi.org/10.1128/mcb.15.10.5288.

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Heat shock factor 2 (HSF2) functions as a transcriptional regulator of heat shock protein gene expression in mammalian cells undergoing processes of differentiation and development. Our previous studies demonstrated high regulated expression and unusual constitutive DNA-binding activity of the HSF2 protein in mouse testes, suggesting that HSF2 functions to regulate heat shock protein gene expression in spermatogenic cells. The purpose of this study was to test whether HSF2 regulation in testes is associated with alterations in the HSF2 polypeptide expressed in testes relative to other mouse tissues. Our results show that mouse cells express not one but two distinct HSF2 proteins and that the levels of these HSF2 isoforms are regulated in a tissue-dependent manner. The testes express predominantly the 71-kDa HSF2-alpha isoform, while the heart and brain express primarily the 69-kDa HSF2-beta isoform. These isoforms are generated by alternative splicing of HSF2 pre-mRNA, which results in the inclusion of an 18-amino-acid coding sequence in the HSF2-alpha mRNA that is skipped in the HSF2-beta mRNA. HSF2 alternative splicing is also developmentally regulated, as our results reveal a switch in expression from the HSF2-beta mRNA isoform to the HSF2-alpha isoform during testis postnatal developmental. Transfection analysis shows that the HSF2-alpha protein, the predominant isoform expressed in testis cells, is a more potent transcriptional activator than the HSF2-beta isoform. These results reveal a new mechanism for the control of HSF2 function in mammalian cells, in which regulated alternative splicing is used to modulate HSF2 transcriptional activity in a tissue-dependent manner.

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Sandqvist, Anton, Johanna K. Björk, Malin Åkerfelt, Zhanna Chitikova, Alexei Grichine, Claire Vourc'h, Caroline Jolly, Tiina A. Salminen, Yvonne Nymalm y Lea Sistonen. "Heterotrimerization of Heat-Shock Factors 1 and 2 Provides a Transcriptional Switch in Response to Distinct Stimuli". Molecular Biology of the Cell 20, n.º 5 (marzo de 2009): 1340–47. http://dx.doi.org/10.1091/mbc.e08-08-0864.

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Organisms respond to circumstances threatening the cellular protein homeostasis by activation of heat-shock transcription factors (HSFs), which play important roles in stress resistance, development, and longevity. Of the four HSFs in vertebrates (HSF1-4), HSF1 is activated by stress, whereas HSF2 lacks intrinsic stress responsiveness. The mechanism by which HSF2 is recruited to stress-inducible promoters and how HSF2 is activated is not known. However, changes in the HSF2 expression occur, coinciding with the functions of HSF2 in development. Here, we demonstrate that HSF1 and HSF2 form heterotrimers when bound to satellite III DNA in nuclear stress bodies, subnuclear structures in which HSF1 induces transcription. By depleting HSF2, we show that HSF1-HSF2 heterotrimerization is a mechanism regulating transcription. Upon stress, HSF2 DNA binding is HSF1 dependent. Intriguingly, when the elevated expression of HSF2 during development is mimicked, HSF2 binds to DNA and becomes transcriptionally competent. HSF2 activation leads to activation of also HSF1, revealing a functional interdependency that is mediated through the conserved trimerization domains of these factors. We propose that heterotrimerization of HSF1 and HSF2 integrates transcriptional activation in response to distinct stress and developmental stimuli.

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Pigłowski, Wojciech, Radosława Nowak, Zdzisław Krawczyk y Dorota Scieglińska. "The structural and functional analysis of the human HSPA2 gene promoter region." Acta Biochimica Polonica 54, n.º 1 (20 de marzo de 2007): 99–106. http://dx.doi.org/10.18388/abp.2007_3274.

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HSPA2 is a human counterpart of the testis-specific rodent Hst70/Hsp70.2 gene. In contrast to the latter, the expression of the human HSPA2 gene is not limited to the testis, and recent data show that human tumor cells can express this gene at significant levels. The characteristics of HSPA2 expression suggests that it can influence the phenotype and survival of cancer cells similarly as overexpression of major members of the HSP70 gene family. Until now, neither the structure of the transcription unit of the human HSPA2 gene has been established nor a functional analysis of its promoter performed. In this study we established that the human HSPA2 gene, in contrast to its rodent counterparts, is intronless and has a single transcription start site. We also show that the same type of HSPA2 transcripts are synthesized in the testes and in cancer cell lines. In order to perform a functional study of the HSPA2 promoter, we used a transient transfection assay and found that the 392 bp fragment upstream of the ATG codon was a minimal region required for efficient transcription, while a 150 bp deletion from the 5' end of this region dramatically reduced the promoter activity. Delineation of the minimal promoter is a basic step toward identifying the cis and trans elements involved in the regulation of the HSPA2 gene expression in cancer cells.

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Scieglinska, Dorota, Damian Robert Sojka, Agnieszka Gogler-Pigłowska, Vira Chumak y Zdzisław Krawczyk. "Various Anti-HSPA2 Antibodies Yield Different Results in Studies on Cancer-Related Functions of Heat Shock Protein A2". International Journal of Molecular Sciences 21, n.º 12 (16 de junio de 2020): 4296. http://dx.doi.org/10.3390/ijms21124296.

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Heat shock proteins (HSPs) constitute a major part of the molecular chaperone system and play a fundamental role in cell proteostasis. The HSPA (HSP70) family groups twelve highly homologous HSPA proteins. Certain HSPAs are regarded as important cancer-related proteins, prospective therapeutic targets for cancer treatment, and also as potential cancer biomarkers. Heat Shock Protein A2 (HSPA2), a testis-enriched chaperone and one of the least characterized members of the HSPA family, has recently emerged as an important cancer-relevant protein with potential biomarker significance. Nevertheless, conflicting conclusions have been recently drawn both according to HSPA2 role in cancer cells, as well as to its prognostic value. In this work we have shown that one of the serious limitations in HSPA2 protein research is cross-reactivity of antibodies marketed as specific for HSPA2 with one or more other HSPA(s). Among non-specific antibodies were also those recently used for HSPA2 detection in functional and biomarker studies. We showed how using non-specific antibodies can generate misleading conclusions on HSPA2 expression in non-stressed cancer cells and tumors, as well as in cancer cells exposed to proteotoxic stress. Our findings addressed concerns on some published studies dealing with HSPA2 as a cancer-related protein.

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Malumpong, C., S. Cheabu, C. Mongkolsiriwatana, W. Detpittayanan y A. Vanavichit. "Spikelet fertility and heat shock transcription factor (Hsf) gene responses to heat stress in tolerant and susceptible rice (Oryza sativa L.) genotypes". Journal of Agricultural Science 157, n.º 04 (mayo de 2019): 283–99. http://dx.doi.org/10.1017/s002185961900056x.

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AbstractThe reproductive stage of rice is the most sensitive to heat stress, which can lead to spikelet sterility. Thus, heat-tolerant and heat-susceptible genotypes were used to investigate their differences in terms of phenotypic responses and expression changes of Hsf genes at the pre-flowering stage under heat stress. Results clearly showed that panicles had the highest temperature compared with other plant parts under both natural and heated conditions. However, the temperatures of tolerant and susceptible genotypes were not significantly different. In terms of spikelet fertility, the tolerant lines M9962 and M7988 had high seed set because their anther dehiscence, pollen viability and pollen germination were only slightly affected. In contrast, the susceptible line Sinlek showed severe effects at all steps of fertilization, and the pollen viability of M7766 was slightly affected under heat stress but was more affected in terms of anther dehiscence and pollen germination. Both susceptible lines showed dramatically decreased seed set. In addition, the expression of six HsfA genes in the flag leaves and spikelets at the R2 stage of plants under heat stress showed different responses. Notably, expression of the HsfA2a gene was predominantly upregulated in the flag leaf and spikelets under heat stress in M9962. Therefore, it can be concluded that heat stress has severe effects on the stamen, and that different genotypes have different susceptibilities to heat stress.

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Shinkawa, Toyohide, Ke Tan, Mitsuaki Fujimoto, Naoki Hayashida, Kaoru Yamamoto, Eiichi Takaki, Ryosuke Takii et al. "Heat shock factor 2 is required for maintaining proteostasis against febrile-range thermal stress and polyglutamine aggregation". Molecular Biology of the Cell 22, n.º 19 (octubre de 2011): 3571–83. http://dx.doi.org/10.1091/mbc.e11-04-0330.

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Heat shock response is characterized by the induction of heat shock proteins (HSPs), which facilitate protein folding, and non-HSP proteins with diverse functions, including protein degradation, and is regulated by heat shock factors (HSFs). HSF1 is a master regulator of HSP expression during heat shock in mammals, as is HSF3 in avians. HSF2 plays roles in development of the brain and reproductive organs. However, the fundamental roles of HSF2 in vertebrate cells have not been identified. Here we find that vertebrate HSF2 is activated during heat shock in the physiological range. HSF2 deficiency reduces threshold for chicken HSF3 or mouse HSF1 activation, resulting in increased HSP expression during mild heat shock. HSF2-null cells are more sensitive to sustained mild heat shock than wild-type cells, associated with the accumulation of ubiquitylated misfolded proteins. Furthermore, loss of HSF2 function increases the accumulation of aggregated polyglutamine protein and shortens the lifespan of R6/2 Huntington's disease mice, partly through αB-crystallin expression. These results identify HSF2 as a major regulator of proteostasis capacity against febrile-range thermal stress and suggest that HSF2 could be a promising therapeutic target for protein-misfolding diseases.

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Mathew, Anu, Sameer K. Mathur y Richard I. Morimoto. "Heat Shock Response and Protein Degradation: Regulation of HSF2 by the Ubiquitin-Proteasome Pathway". Molecular and Cellular Biology 18, n.º 9 (1 de septiembre de 1998): 5091–98. http://dx.doi.org/10.1128/mcb.18.9.5091.

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ABSTRACT Mammalian cells coexpress a family of heat shock factors (HSFs) whose activities are regulated by diverse stress conditions to coordinate the inducible expression of heat shock genes. Distinct from HSF1, which is expressed ubiquitously and activated by heat shock and other stresses that result in the appearance of nonnative proteins, the stress signal for HSF2 has not been identified. HSF2 activity has been associated with development and differentiation, and the activation properties of HSF2 have been characterized in hemin-treated human K562 erythroleukemia cells. Here, we demonstrate that a stress signal for HSF2 activation occurs when the ubiquitin-proteasome pathway is inhibited. HSF2 DNA-binding activity is induced upon exposure of mammalian cells to the proteasome inhibitors hemin, MG132, and lactacystin, and in the mouse ts85 cell line, which carries a temperature sensitivity mutation in the ubiquitin-activating enzyme (E1) upon shift to the nonpermissive temperature. HSF2 is labile, and its activation requires both continued protein synthesis and reduced degradation. The downstream effect of HSF2 activation by proteasome inhibitors is the induction of the same set of heat shock genes that are induced during heat shock by HSF1, thus revealing that HSF2 affords the cell with a novel heat shock gene-regulatory mechanism to respond to changes in the protein-degradative machinery.

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McMillan, D. Randy, Elisabeth Christians, Michael Forster, XianZhong Xiao, Patrice Connell, Jean-Christophe Plumier, XiaoXia Zuo, James Richardson, Sylvia Morgan y Ivor J. Benjamin. "Heat Shock Transcription Factor 2 Is Not Essential for Embryonic Development, Fertility, or Adult Cognitive and Psychomotor Function in Mice". Molecular and Cellular Biology 22, n.º 22 (15 de noviembre de 2002): 8005–14. http://dx.doi.org/10.1128/mcb.22.22.8005-8014.2002.

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ABSTRACT Members of the heat shock factor (HSF) family are evolutionarily conserved regulators that share a highly homologous DNA-binding domain. In mammals, HSF1 is the main factor controlling the stress-inducible expression of Hsp genes while the functions of HSF2 and HSF4 are less clear. Based on its developmental profile of expression, it was hypothesized that HSF2 may play an essential role in brain and heart development, spermatogenesis, and erythroid differentiation. To directly assess this hypothesis and better understand the underlying mechanisms that require HSF2, we generated Hsf2 knockout mice. Here, we report that Hsf2 −/− mice are viable and fertile and exhibit normal life span and behavioral functions. We conclude that HSF2, most probably because its physiological roles are integrated into a redundant network of gene regulation and function, is dispensable for normal development, fertility, and postnatal psychomotor function.