Cloning and identification of grass carp transcription factor HSF1 and its characterization involving the production of fish HSP70

Yang, Xinrui; Gao, Yajun; Zhao, Minghui; Wang, Xinyan; Zhou, Hong; Zhang, Anying

doi:10.1007/s10695-020-00842-4

Cited by 5 publications

(6 citation statements)

References 66 publications

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“…By expressing HSP70 in goldfish and pollack, as well as various other fish, we found that HSF1 can bind to the DBD. 25,39,42,46,52,53 However, further analysis of the HSF1 mutations in fish is needed. Although we confirmed trimer formation of the HSF1 mutant in vitro, additional experiments should be performed to determine whether the mutant binds to the DBD in vivo.…”

Section: Discussionmentioning

confidence: 99%

“…Studies have been conducted on the HSF1s of various species including humans, mice, chicken, goldfish, and carp. All of these various types of HSF1s are activated by binding to HSEs. ,− The focus of this study was to investigate the trimerization of human, goldfish, and walleye pollock HSF1 at different temperatures and to elucidate the trimerization mechanism. A previous study has shown that hHSF1 is characterized by two cysteines located in the DBD that are bonded via disulfide bonds and that it has a high trimerization temperature of approximately 42 °C. ,, Meanwhile, previous studies have shown that gHSF1 lacks disulfide bonds and that trimerization occurs at approximately 37 °C .…”

Section: Discussionmentioning

confidence: 99%

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Intermolecular Interactions between Cysteine and Aromatic Amino Acids with a Phenyl Moiety in the DNA-Binding Domain of Heat Shock Factor 1 Regulate Thermal Stress-Induced Trimerization

Lee,

Choi,

Kim

et al. 2024

Biochemistry

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In this study, we investigated the trimerization mechanism and structure of heat shock factor 1 (HSF1) using western blotting, tryptophan (Trp) fluorescence spectroscopy, and molecular modeling. First, we examined the DNA-binding domains of human (Homo sapiens), goldfish (Carassius auratus), and walleye pollock (Gadus chalcogrammus) HSF1s by mutating key residues (36 and 103) that are thought to directly affect trimer formation. Human, goldfish, and walleye pollock HSF1s contain cysteine at residue 36 but cysteine (C), tyrosine (Y), and phenylalanine (F), respectively, at residue 103. The optimal trimerization temperatures for the wild-type HSF1s of each species were found to be 42, 37, and 20 °C, respectively. Interestingly, a mutation experiment revealed that trimerization occurred at 42 °C when residue 103 was cysteine, at 37 °C when it was tyrosine, and at 20 °C when it was phenylalanine, regardless of the species. In addition, it was confirmed that when residue 103 of the three species was mutated to alanine, trimerization did not occur. This suggests that in addition to trimerization via disulfide bond formation between the cysteine residues in human HSF1, trimerization can also occur via the formation of a different type of bond between cysteine and aromatic ring residues such as tyrosine and phenylalanine. We also confirmed that at least one cysteine is required for the trimerization of HSF1s, regardless of its position (residue 36 or 103). Additionally, it was shown that the trimer formation temperature is related to growth and survival in fish.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Intermolecular Interactions between Cysteine and Aromatic Amino Acids with a Phenyl Moiety in the DNA-Binding Domain of Heat Shock Factor 1 Regulate Thermal Stress-Induced Trimerization

Lee,

Choi,

Kim

et al. 2024

Biochemistry

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“…HSF1 studies in many species have continued. (human, mouse, chicken, goldfish, carp) [20][21][22][23][24][25] . The focus of this study was the trimerization of human, goldfish, and walleye pollock HSF1 at different temperatures and the mechanism of this trimerization.…”

Section: Discussionmentioning

confidence: 99%

Intermolecular interactions between cysteine and aromatic amino acids with phenyl moiety in the DNA-binding domain of heat shock factor 1 regulate thermal stress-induced trimerization

Lee,

Choi,

So-Sun-Kim

et al. 2023

Preprint

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In this study, we investigated the trimerization mechanism and structure of heat shock factor 1 (HSF1) in humans, goldfish, and walleye pollock at various temperatures. The trimerization of HSF1s were confirmed using western blotting using their respective antibodies. First, we examined the HSF1 DNA-binding domains of human (Homo sapiens), goldfish (Carassius auratus), and walleye pollock (Gadus chalcogrammus) by mutating key residues (36 and 103) that are thought to directly affect trimer generation. Humans, goldfish, and walleye pollock contain cysteine at residue 36, but cysteine (C), tyrosine (Y), and phenylalanine (F) at residue 103. Also, the trimer formation temperature of each species was found to be 42, 37, and 20 °C, respectively. In the mutation experiment, trimerization formed at 42 °C when residue 103 was C, at 37 °C it was Y, and at 20 °C it was F, regardless of the species. In addition, it was confirmed that when residue 103 of the three species was mutated to alanine (A), trimer was not formed. This suggest that, in addition to the previously identified C-C disulfide bonds in humans, C forms a trimer with a new type of bond with aromatic ring residues such as Y and F. Thus, HSF1 trimer formation temperature reveals the trimer creation mechanism through the fact that goldfish can have C-Y bonds at 37 °C, and walleye pollock can have C-F bonds at 20 °C. This study suggests that the trimer formation temperature and mechanism of HSF1 are regulated by the amino acid at residue 103.

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“…The expression of Hsp70 is dependent on Hsf1, which binds to the promoter region of the Hsp70 gene and enhances its transcription ( Calderwood et al, 2010 ; Wu, 1995 ). Interestingly, both Hsf1 and Hsp70 play a protective role in organisms in response to stressful conditions ( Doubrovin et al, 2012 ; Lin et al, 2016 ; Peng et al, 2010 ; Yang et al, 2020 ). Accordingly, several studies have evaluated the changes in Hsf1 and Hsp70 expression in model animals under hypoxic stress.…”

Section: Discussionmentioning

confidence: 99%

“…In human articular chondrocytes under hypoxic stress, Hif-1α induces a significant increase in the expression of both Hsp70 mRNA and protein ( Tsuchida et al, 2014 ). The transcription of Hsp70 mRNA is primarily mediated by Hsf1 ( Doubrovin et al, 2012 ; Lin et al, 2016 ; Peng et al, 2010 ; Yang et al, 2020 ). Accordingly, several studies have explored the transcriptional regulation of Hif-1α, Hsf1, and Hsp70 under hypoxic stress.…”

Section: Discussionmentioning

confidence: 99%

Hif-1α/Hsf1/Hsp70 signaling pathway regulates redox homeostasis and apoptosis in large yellow croaker (<i>Larimichthys crocea</i>) under environmental hypoxia

Luo

Wang

Liu

et al. 2021

Zoological Research

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Oxygen is an essential molecule for animal respiration, growth, and survival. Unlike in terrestrial environments, contamination and climate change have led to the frequent occurrence of hypoxia in aquatic environments, thus impacting aquatic animal survival. However, the adaptative mechanisms underlying fish responses to environmental hypoxia remain largely unknown. Here, we used large yellow croaker ( Larimichthys crocea ) and large yellow croaker fry (LYCF) cells to investigate the roles of the Hif-1α/Hsf1/Hsp70 signaling pathway in the regulation of cellular redox homeostasis, and apoptosis. We confirmed that hypoxia induced the expression of Hif-1α, Hsf1, and Hsp70 in vivo and in vitro . Genetic Hsp70 knockdown/overexpression indicated that Hsp70 was required for maintaining redox homeostasis and resisting oxidative stress in LYCF cells under hypoxic stress. Hsp70 inhibited caspase-dependent intrinsic apoptosis by maintaining normal mitochondrial membrane potential, enhancing Bcl-2 mRNA and protein expression, inhibiting Bax and caspase3 mRNA expression, and suppressing caspase-3 and caspase-9 activation. Hsp70 suppressed caspase-independent intrinsic apoptosis by inhibiting nuclear translocation of apoptosis-inducing factor (AIF) and disturbed extrinsic apoptosis by inactivating caspase-8. Genetic knockdown/overexpression of Hif-1α and dual-luciferase reporter assay indicated that Hif-1α activated the Hsf1 DNA promoter and enhanced Hsf1 mRNA transcription. Hsf1 enhanced Hsp70 mRNA transcription in a similar manner. In summary, the Hif-1α/Hsf1/Hsp70 signaling pathway plays an important role in regulating redox homeostasis and anti-apoptosis in L. crocea under hypoxic stress.

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Cloning and identification of grass carp transcription factor HSF1 and its characterization involving the production of fish HSP70

Cited by 5 publications

References 66 publications

Intermolecular Interactions between Cysteine and Aromatic Amino Acids with a Phenyl Moiety in the DNA-Binding Domain of Heat Shock Factor 1 Regulate Thermal Stress-Induced Trimerization

Intermolecular Interactions between Cysteine and Aromatic Amino Acids with a Phenyl Moiety in the DNA-Binding Domain of Heat Shock Factor 1 Regulate Thermal Stress-Induced Trimerization

Intermolecular interactions between cysteine and aromatic amino acids with phenyl moiety in the DNA-binding domain of heat shock factor 1 regulate thermal stress-induced trimerization

Hif-1α/Hsf1/Hsp70 signaling pathway regulates redox homeostasis and apoptosis in large yellow croaker (<i>Larimichthys crocea</i>) under environmental hypoxia

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