Heat Shock Protein 70 Family in Response to Multiple Abiotic Stresses in the Silkworm

The 70 kDa heat shock proteins play important roles in protecting organisms against environmental stresses, which are divided into stress-inducible forms (HSP70s) and heat shock cognates (HSC70s). In this study, heat shock protein 70 family was identified in the whole genome of the silkworm. Based o...

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Published inInsects (Basel, Switzerland) Vol. 12; no. 10; p. 928
Main Authors Fang, Shou-Min, Zhang, Qian, Zhang, Yu-Li, Zhang, Gui-Zheng, Zhang, Ze, Yu, Quan-You
Format Journal Article
LanguageEnglish
Published Basel MDPI AG 12.10.2021
MDPI
Subjects
Adaptation
Biopolymer denaturation
Bombyx mori
Cold
Dichlorvos
Drinking water
Environmental stress
Fat body
Genes
genome-wide
Genomes
Genomics
Heat
heat shock protein 70
Heat shock proteins
heat stress
Hsc70 protein
Hsp70 protein
Insecticides
Insects
Larvae
Midgut
Pesticide pollution
Pesticides
Phoxim
Phylogenetics
Phylogeny
Protein denaturation
Protein folding
silkworm
Silkworms
stress response
Thermal stress
Transcription
Beijing China
United States > US
China
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Abstract The 70 kDa heat shock proteins play important roles in protecting organisms against environmental stresses, which are divided into stress-inducible forms (HSP70s) and heat shock cognates (HSC70s). In this study, heat shock protein 70 family was identified in the whole genome of the silkworm. Based on the known nomenclature and phylogenetic analysis, four HSP70s and five HSC70s were classified. Relatively, heat shock cognates were more conservative and were constitutively expressed in various tissues of the silkworm larvae. Under thermal (37 °C and 42 °C) and cold (2 °C) stresses, the expressions of HSP70–1, HSP70–2, and HSP70–3 were up-regulated, and the highest induction reached 4147.3, 607.1, and 1987.3 times, respectively. Interestingly, HSC70–1, HSC70–4, and HSC70–5 also showed slight induced expressions in the fat body and/or midgut under thermal stresses. In addition, the expression of HSP70–1 was induced by dichlorvos and phoxim insecticides, while most HSC70 genes were inhibited. The results suggested that stress-inducible forms play more important roles in adaptation to various stresses than HSC70s.
AbstractList The 70 kDa heat shock proteins play important roles in protecting organisms against environmental stresses, which are divided into stress-inducible forms (HSP70s) and heat shock cognates (HSC70s). In this study, heat shock protein 70 family was identified in the whole genome of the silkworm. Based on the known nomenclature and phylogenetic analysis, four HSP70s and five HSC70s were classified. Relatively, heat shock cognates were more conservative and were constitutively expressed in various tissues of the silkworm larvae. Under thermal (37 °C and 42 °C) and cold (2 °C) stresses, the expressions of HSP70-1, HSP70-2, and HSP70-3 were up-regulated, and the highest induction reached 4147.3, 607.1, and 1987.3 times, respectively. Interestingly, HSC70-1, HSC70-4, and HSC70-5 also showed slight induced expressions in the fat body and/or midgut under thermal stresses. In addition, the expression of HSP70-1 was induced by dichlorvos and phoxim insecticides, while most HSC70 genes were inhibited. The results suggested that stress-inducible forms play more important roles in adaptation to various stresses than HSC70s.The 70 kDa heat shock proteins play important roles in protecting organisms against environmental stresses, which are divided into stress-inducible forms (HSP70s) and heat shock cognates (HSC70s). In this study, heat shock protein 70 family was identified in the whole genome of the silkworm. Based on the known nomenclature and phylogenetic analysis, four HSP70s and five HSC70s were classified. Relatively, heat shock cognates were more conservative and were constitutively expressed in various tissues of the silkworm larvae. Under thermal (37 °C and 42 °C) and cold (2 °C) stresses, the expressions of HSP70-1, HSP70-2, and HSP70-3 were up-regulated, and the highest induction reached 4147.3, 607.1, and 1987.3 times, respectively. Interestingly, HSC70-1, HSC70-4, and HSC70-5 also showed slight induced expressions in the fat body and/or midgut under thermal stresses. In addition, the expression of HSP70-1 was induced by dichlorvos and phoxim insecticides, while most HSC70 genes were inhibited. The results suggested that stress-inducible forms play more important roles in adaptation to various stresses than HSC70s.
The 70 kDa heat shock proteins play important roles in protecting organisms against environmental stresses, which are divided into stress-inducible forms (HSP70s) and heat shock cognates (HSC70s). In this study, heat shock protein 70 family was identified in the whole genome of the silkworm. Based on the known nomenclature and phylogenetic analysis, four HSP70s and five HSC70s were classified. Relatively, heat shock cognates were more conservative and were constitutively expressed in various tissues of the silkworm larvae. Under thermal (37 °C and 42 °C) and cold (2 °C) stresses, the expressions of HSP70–1, HSP70–2, and HSP70–3 were up-regulated, and the highest induction reached 4147.3, 607.1, and 1987.3 times, respectively. Interestingly, HSC70–1, HSC70–4, and HSC70–5 also showed slight induced expressions in the fat body and/or midgut under thermal stresses. In addition, the expression of HSP70–1 was induced by dichlorvos and phoxim insecticides, while most HSC70 genes were inhibited. The results suggested that stress-inducible forms play more important roles in adaptation to various stresses than HSC70s.
Simple SummaryHeat shock protein 70 family is widely distributed in all the organisms, which plays important roles in protein folding and preventing protein denaturation. Heat or cold stress response has been studied in some insects, but there is a lack of systematic investigation on the response of the same species to multiple stressors. Here, we performed genome-wide identification of heat shock protein 70 family in the silkworm, Bombyx mori. Using the silkworm as a model, the transcription profiles of all the genes against heat, cold, and pesticides were studied. Our findings would provide insights into the functional diversification of heat shock proteins 70 in insects.AbstractThe 70 kDa heat shock proteins play important roles in protecting organisms against environmental stresses, which are divided into stress-inducible forms (HSP70s) and heat shock cognates (HSC70s). In this study, heat shock protein 70 family was identified in the whole genome of the silkworm. Based on the known nomenclature and phylogenetic analysis, four HSP70s and five HSC70s were classified. Relatively, heat shock cognates were more conservative and were constitutively expressed in various tissues of the silkworm larvae. Under thermal (37 °C and 42 °C) and cold (2 °C) stresses, the expressions of HSP70–1, HSP70–2, and HSP70–3 were up-regulated, and the highest induction reached 4147.3, 607.1, and 1987.3 times, respectively. Interestingly, HSC70–1, HSC70–4, and HSC70–5 also showed slight induced expressions in the fat body and/or midgut under thermal stresses. In addition, the expression of HSP70–1 was induced by dichlorvos and phoxim insecticides, while most HSC70 genes were inhibited. The results suggested that stress-inducible forms play more important roles in adaptation to various stresses than HSC70s.
Author Zhang, Ze
Zhang, Qian
Fang, Shou-Min
Zhang, Yu-Li
Yu, Quan-You
Zhang, Gui-Zheng
AuthorAffiliation 2 College of Life Science, China West Normal University, Nanchong 637002, China
1 School of Life Sciences, Chongqing University, Chongqing 400044, China; fangshoumin@126.com (S.-M.F.); zhangqiankobe24@163.com (Q.Z.); zezhang@cqu.edu.cn (Z.Z.)
3 Guangxi Academy of Sericultural Sciences, Nanning 530007, China; ZYL8324@126.com (Y.-L.Z.); zhangdoudou1999@163.com (G.-Z.Z.)
AuthorAffiliation_xml – name: 3 Guangxi Academy of Sericultural Sciences, Nanning 530007, China; ZYL8324@126.com (Y.-L.Z.); zhangdoudou1999@163.com (G.-Z.Z.)
– name: 1 School of Life Sciences, Chongqing University, Chongqing 400044, China; fangshoumin@126.com (S.-M.F.); zhangqiankobe24@163.com (Q.Z.); zezhang@cqu.edu.cn (Z.Z.)
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Cites_doi 10.1007/s11356-017-9898-0
10.1007/s12192-019-00983-3
10.1016/j.tox.2007.09.029
10.1002/jbt.10086
10.1186/1471-2164-8-231
10.1242/jcs.110.13.1431
10.1016/S0960-9822(00)00249-9
10.1111/1744-7917.12505
10.1017/S0007485320000541
10.1016/j.jinsphys.2014.06.009
10.7717/peerj.7511
10.1111/j.1601-5223.1999.00155.x
10.2174/138920208785133280
10.1146/annurev.cb.09.110193.003125
10.1146/annurev.physiol.61.1.243
10.1146/annurev-ento-011613-161940
10.1016/j.lfs.2009.12.015
10.1186/1471-2105-11-431
10.1016/j.bbagen.2007.05.010
10.1016/j.ygeno.2020.07.039
10.1186/1741-7007-6-5
10.1074/jbc.REV118.002810
10.1016/j.chemosphere.2010.01.054
10.1242/jeb.02695
10.1111/j.1742-4658.2009.07470.x
10.1603/EC10260
10.1016/j.tox.2007.05.017
10.1073/pnas.0703538104
10.1046/j.1461-0248.2003.00528.x
10.1016/j.cbpc.2008.07.009
10.1046/j.1365-294X.2002.01882.x
10.1371/journal.pone.0004546
10.1006/meth.2001.1262
10.1016/j.pestbp.2017.01.011
10.1093/nar/25.24.4876
10.1016/S0163-7258(98)00028-X
10.1016/j.fsi.2011.04.015
10.1093/molbev/msu300
10.1172/JCI200318022
10.1002/9780470061619
10.1673/031.010.20401
10.1016/S0306-4565(02)00057-8
10.1016/j.jtherbio.2019.07.005
10.1016/S0021-9258(19)38314-0
10.1016/j.chemosphere.2012.06.028
10.1016/0092-8674(94)90416-2
10.1111/evo.14025
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References Singh (ref_50) 2010; 79
Xia (ref_39) 2014; 59
Marnett (ref_49) 2003; 111
Saradha (ref_46) 2008; 243
Manjunatha (ref_48) 2010; 10
Garcia (ref_19) 2020; 74
ref_11
Li (ref_42) 2021; 111
Gupta (ref_24) 2007; 238
ref_15
Lu (ref_43) 2020; 48
Hoffmann (ref_3) 2003; 28
Colinet (ref_22) 2010; 277
Craig (ref_8) 1994; 78
Hu (ref_12) 2014; 67
Schlesinger (ref_7) 1990; 265
ref_23
Georgopoulos (ref_5) 1993; 9
Rehman (ref_32) 2020; 112
Howrelia (ref_47) 2011; 32
Ilijin (ref_25) 2017; 24
Gupta (ref_26) 2007; 1770
Yu (ref_40) 2011; 104
Dumas (ref_20) 2019; 24
Xing (ref_27) 2013; 90
Sorensen (ref_14) 1999; 131
Livak (ref_41) 2001; 25
Kabani (ref_34) 2008; 9
ref_36
ref_35
Sorensen (ref_10) 2019; 84
Mukhopadhyay (ref_31) 2003; 17
Gupta (ref_45) 1994; 4
Lu (ref_17) 2017; 142
Kiang (ref_44) 1998; 80
Frydenberg (ref_2) 2003; 12
Wang (ref_28) 2011; 31
Liang (ref_6) 1997; 110
Wang (ref_13) 2019; 26
Sorensen (ref_4) 2003; 6
Nguyen (ref_38) 2015; 32
Mayer (ref_9) 2019; 294
Liang (ref_33) 2019; 7
Thompson (ref_37) 1997; 25
Gupta (ref_29) 2010; 86
Burton (ref_21) 1988; 8
Feder (ref_1) 1999; 61
Rhee (ref_30) 2009; 149
Rinehart (ref_18) 2007; 104
Rank (ref_16) 2007; 210
References_xml – volume: 32
  start-page: 99
  year: 2011
  ident: ref_47
  article-title: Impact of temperature on heat shock protein expression of Bombyx mori cross-breed and effect on commercial traits
  publication-title: J. Environ. Biol.
– volume: 24
  start-page: 20818
  year: 2017
  ident: ref_25
  article-title: Acetylcholinesterase and heat shock protein 70 response in larval brain tissue of Lymantria dispar L. (Lepidoptera, Limantriidae) upon chronic exposure to benzo(a)pyrene
  publication-title: Environ. Sci. Pollut. Res. Int.
  doi: 10.1007/s11356-017-9898-0
– volume: 24
  start-page: 539
  year: 2019
  ident: ref_20
  article-title: Expression status of heat shock proteins in response to cold, heat, or insecticide exposure in the Colorado potato beetle Leptinotarsa decemlineata
  publication-title: Cell Stress Chaperones
  doi: 10.1007/s12192-019-00983-3
– volume: 243
  start-page: 116
  year: 2008
  ident: ref_46
  article-title: Lindane alters the levels of HSP70 and clusterin in adult rat testis
  publication-title: Toxicology
  doi: 10.1016/j.tox.2007.09.029
– volume: 17
  start-page: 249
  year: 2003
  ident: ref_31
  article-title: Heat shock response: Hsp70 in environmental monitoring
  publication-title: J. Biochem. Mol. Toxicol.
  doi: 10.1002/jbt.10086
– ident: ref_15
  doi: 10.1186/1471-2164-8-231
– volume: 110
  start-page: 1431
  year: 1997
  ident: ref_6
  article-title: Molecular chaperones and the cytoskeleton
  publication-title: J. Cell Sci.
  doi: 10.1242/jcs.110.13.1431
– volume: 4
  start-page: 1104
  year: 1994
  ident: ref_45
  article-title: Phylogenetic analysis of 70 kD heat shock protein sequences suggests a chimeric origin for the eukaryotic cell nucleus
  publication-title: Curr. Biol.
  doi: 10.1016/S0960-9822(00)00249-9
– volume: 26
  start-page: 44
  year: 2019
  ident: ref_13
  article-title: Genome-wide identification and characterization of HSP gene superfamily in whitefly (Bemisia tabaci) and expression profiling analysis under temperature stress
  publication-title: Insect Sci.
  doi: 10.1111/1744-7917.12505
– volume: 111
  start-page: 217
  year: 2021
  ident: ref_42
  article-title: Characterization, expression profiling, and thermal tolerance analysis of heat shock protein 70 in pine sawyer beetle, Monochamus alternatus hope (Coleoptera: Cerambycidae)
  publication-title: Bull. Entomol. Res.
  doi: 10.1017/S0007485320000541
– volume: 67
  start-page: 105
  year: 2014
  ident: ref_12
  article-title: Thermal plasticity is related to the hardening response of heat shock protein expression in two Bactrocera fruit flies
  publication-title: J. Insect Physiol.
  doi: 10.1016/j.jinsphys.2014.06.009
– volume: 7
  start-page: e7511
  year: 2019
  ident: ref_33
  article-title: Genome-wide identification and characterization of the Hsp70 gene family in allopolyploid rapeseed (Brassica napus L.) compared with its diploid progenitors
  publication-title: PeerJ
  doi: 10.7717/peerj.7511
– volume: 131
  start-page: 155
  year: 1999
  ident: ref_14
  article-title: Expression of the heat-shock protein HSP70 in Drosophila buzzatii lines selected for thermal resistance
  publication-title: Hereditas
  doi: 10.1111/j.1601-5223.1999.00155.x
– volume: 9
  start-page: 338
  year: 2008
  ident: ref_34
  article-title: Multiple hsp70 isoforms in the eukaryotic cytosol: Mere redundancy or functional specificity?
  publication-title: Curr. Genomics
  doi: 10.2174/138920208785133280
– volume: 9
  start-page: 601
  year: 1993
  ident: ref_5
  article-title: Role of the major heat-shock proteins as molecular chaperones
  publication-title: Annu. Rev. Cell Biol.
  doi: 10.1146/annurev.cb.09.110193.003125
– volume: 61
  start-page: 243
  year: 1999
  ident: ref_1
  article-title: Heat-shock proteins, molecular chaperones, and the stress response: Evolutionary and ecological physiology
  publication-title: Annu. Rev. Physiol.
  doi: 10.1146/annurev.physiol.61.1.243
– volume: 59
  start-page: 513
  year: 2014
  ident: ref_39
  article-title: Advances in silkworm studies accelerated by the genome sequencing of Bombyx mori
  publication-title: Annu Rev Entomol.
  doi: 10.1146/annurev-ento-011613-161940
– volume: 86
  start-page: 377
  year: 2010
  ident: ref_29
  article-title: Heat shock proteins in toxicology: How close and how far?
  publication-title: Life Sci.
  doi: 10.1016/j.lfs.2009.12.015
– ident: ref_35
  doi: 10.1186/1471-2105-11-431
– volume: 1770
  start-page: 1382
  year: 2007
  ident: ref_26
  article-title: Induction of hsp70, alterations in oxidative stress markers and apoptosis against dichlorvos exposure in transgenic Drosophila melanogaster: Modulation by reactive oxygen species
  publication-title: Biochim. Biophys. Acta
  doi: 10.1016/j.bbagen.2007.05.010
– volume: 112
  start-page: 4442
  year: 2020
  ident: ref_32
  article-title: Genome-wide identification and characterization of HSP70 gene family in four species of cotton
  publication-title: Genomics
  doi: 10.1016/j.ygeno.2020.07.039
– ident: ref_11
  doi: 10.1186/1741-7007-6-5
– volume: 294
  start-page: 2085
  year: 2019
  ident: ref_9
  article-title: Recent advances in the structural and mechanistic aspects of Hsp70 molecular chaperones
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.REV118.002810
– volume: 79
  start-page: 577
  year: 2010
  ident: ref_50
  article-title: Effects of co-exposure of benzene, toluene and xylene to Drosophila melanogaster: Alteration in hsp70, hsp60, hsp83, hsp26, ROS generation and oxidative stress markers
  publication-title: Chemosphere
  doi: 10.1016/j.chemosphere.2010.01.054
– volume: 8
  start-page: 3550
  year: 1988
  ident: ref_21
  article-title: Heat shock protection against cold stress of Drosophila melanogaster
  publication-title: Mol. Cell Biol.
– volume: 210
  start-page: 750
  year: 2007
  ident: ref_16
  article-title: Phosphoglucose isomerase genotype affects running speed and heat shock protein expression after exposure to extreme temperatures in a montane willow beetle
  publication-title: J. Exp. Biol.
  doi: 10.1242/jeb.02695
– volume: 277
  start-page: 174
  year: 2010
  ident: ref_22
  article-title: Temporal expression of heat shock genes during cold stress and recovery from chill coma in adult Drosophila melanogaster
  publication-title: FEBS J.
  doi: 10.1111/j.1742-4658.2009.07470.x
– volume: 104
  start-page: 101
  year: 2011
  ident: ref_40
  article-title: Effect of organophosphate phoxim exposure on certain oxidative stress biomarkers in the silkworm
  publication-title: J. Econ. Entomol.
  doi: 10.1603/EC10260
– volume: 238
  start-page: 1
  year: 2007
  ident: ref_24
  article-title: Adverse effect of organophosphate compounds, dichlorvos and chlorpyrifos in the reproductive tissues of transgenic Drosophila melanogaster: 70kDa heat shock protein as a marker of cellular damage
  publication-title: Toxicology
  doi: 10.1016/j.tox.2007.05.017
– volume: 104
  start-page: 11130
  year: 2007
  ident: ref_18
  article-title: Up-regulation of heat shock proteins is essential for cold survival during insect diapause
  publication-title: Proc. Natl. Acad. Sci. USA
  doi: 10.1073/pnas.0703538104
– volume: 6
  start-page: 1025
  year: 2003
  ident: ref_4
  article-title: The evolutionary and ecological role of heat shock proteins
  publication-title: Ecol. Lett.
  doi: 10.1046/j.1461-0248.2003.00528.x
– volume: 149
  start-page: 104
  year: 2009
  ident: ref_30
  article-title: Heat shock protein (Hsp) gene responses of the intertidal copepod Tigriopus japonicus to environmental toxicants
  publication-title: Comp. Biochem. Physiol. C Toxicol. Pharmacol.
  doi: 10.1016/j.cbpc.2008.07.009
– volume: 12
  start-page: 2025
  year: 2003
  ident: ref_2
  article-title: DNA sequence variation and latitudinal associations in hsp23, hsp26 and hsp27 from natural populations of Drosophila melanogaster
  publication-title: Mol. Ecol.
  doi: 10.1046/j.1365-294X.2002.01882.x
– ident: ref_23
  doi: 10.1371/journal.pone.0004546
– volume: 25
  start-page: 402
  year: 2001
  ident: ref_41
  article-title: Analysis of relative gene expression data using real-time quantitative PCR and the 2(T)(-Delta Delta C) method
  publication-title: Methods
  doi: 10.1006/meth.2001.1262
– volume: 142
  start-page: 102
  year: 2017
  ident: ref_17
  article-title: Characterization of heat shock protein 70 transcript from Nilaparvata lugens (Stal): Its response to temperature and insecticide stresses
  publication-title: Pestic. Biochem. Physiol.
  doi: 10.1016/j.pestbp.2017.01.011
– volume: 25
  start-page: 4876
  year: 1997
  ident: ref_37
  article-title: The CLUSTAL_X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
  publication-title: Nucleic. Acids Res.
  doi: 10.1093/nar/25.24.4876
– volume: 80
  start-page: 183
  year: 1998
  ident: ref_44
  article-title: Heat shock protein 70 kDa: Molecular biology, biochemistry, and physiology
  publication-title: Pharmacol. Ther.
  doi: 10.1016/S0163-7258(98)00028-X
– volume: 31
  start-page: 126
  year: 2011
  ident: ref_28
  article-title: Effects of atrazine and chlorpyrifos on the mRNA levels of IL-1 and IFN-gamma2b in immune organs of common carp
  publication-title: Fish Shellfish Immunol.
  doi: 10.1016/j.fsi.2011.04.015
– volume: 32
  start-page: 268
  year: 2015
  ident: ref_38
  article-title: IQ-TREE: A Fast and effective stochastic algorithm for estimating maximum-likelihood phylogenies
  publication-title: Mol. Biol. Evol.
  doi: 10.1093/molbev/msu300
– volume: 48
  start-page: D749
  year: 2020
  ident: ref_43
  article-title: SilkDB 3.0: Visualizing and exploring multiple levels of data for silkworm
  publication-title: Nucleic. Acids Res.
– volume: 111
  start-page: 583
  year: 2003
  ident: ref_49
  article-title: Endogenous generation of reactive oxidants and electrophiles and their reactions with DNA and protein
  publication-title: J. Clin. Investig.
  doi: 10.1172/JCI200318022
– ident: ref_36
  doi: 10.1002/9780470061619
– volume: 10
  start-page: 204
  year: 2010
  ident: ref_48
  article-title: Silkworm thermal biology: A review of heat shock response, heat shock proteins and heat acclimation in the domesticated silkworm, Bombyx mori
  publication-title: J. Insect Sci.
  doi: 10.1673/031.010.20401
– volume: 28
  start-page: 175
  year: 2003
  ident: ref_3
  article-title: Adaptation of Drosophila to temperature extremes: Bringing together quantitative and molecular approaches
  publication-title: J. Therm. Biol.
  doi: 10.1016/S0306-4565(02)00057-8
– volume: 84
  start-page: 200
  year: 2019
  ident: ref_10
  article-title: Expression of thermal tolerance genes in two Drosophila species with different acclimation capacities
  publication-title: J. Therm. Biol.
  doi: 10.1016/j.jtherbio.2019.07.005
– volume: 265
  start-page: 12111
  year: 1990
  ident: ref_7
  article-title: Heat-shock proteins
  publication-title: J. Biol. Chem.
  doi: 10.1016/S0021-9258(19)38314-0
– volume: 90
  start-page: 910
  year: 2013
  ident: ref_27
  article-title: Effects of atrazine and chlorpyrifos on the mRNA levels of HSP70 and HSC70 in the liver, brain, kidney and gill of common carp (Cyprinus carpio L.)
  publication-title: Chemosphere
  doi: 10.1016/j.chemosphere.2012.06.028
– volume: 78
  start-page: 365
  year: 1994
  ident: ref_8
  article-title: Heat-shock proteins and molecular chaperones: Mediators of protein conformation and turnover in the cell
  publication-title: Cell
  doi: 10.1016/0092-8674(94)90416-2
– volume: 74
  start-page: 1437
  year: 2020
  ident: ref_19
  article-title: Distinct cold tolerance traits independently vary across genotypes in Drosophila melanogaster
  publication-title: Evol.
  doi: 10.1111/evo.14025
SSID ssj0000612168
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Snippet The 70 kDa heat shock proteins play important roles in protecting organisms against environmental stresses, which are divided into stress-inducible forms...
Simple SummaryHeat shock protein 70 family is widely distributed in all the organisms, which plays important roles in protein folding and preventing protein...
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pubmedcentral
proquest
crossref
SourceType Open Website
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StartPage 928
SubjectTerms Adaptation
Biopolymer denaturation
Bombyx mori
Cold
Dichlorvos
Drinking water
Environmental stress
Fat body
Genes
genome-wide
Genomes
Genomics
Heat
heat shock protein 70
Heat shock proteins
heat stress
Hsc70 protein
Hsp70 protein
Insecticides
Insects
Larvae
Midgut
Pesticide pollution
Pesticides
Phoxim
Phylogenetics
Phylogeny
Protein denaturation
Protein folding
silkworm
Silkworms
stress response
Thermal stress
Transcription
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Title Heat Shock Protein 70 Family in Response to Multiple Abiotic Stresses in the Silkworm
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