Hemin-induced transcriptional activation of the HSP70 gene during erythroid maturation in K562 cells is due to a heat shock factor-mediated stress response.

Theodorakis, Nicholas D.; Zand, Dina J.; Kotzbauer, Paul T.; Williams, Grant; Morimoto, Richard I.

doi:10.1128/mcb.9.8.3166

Cited by 88 publications

(54 citation statements)

References 35 publications

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“…The time-frame for hemin to exhibit profound RNA-stabilization effect coincides with the time required for differentiation of K562 cells further toward erythrocytes (Baliga et al 1993;Nakajima et al 1997). In addition, hemin is known to induce stress response in K562 cells that leads to some significant changes of gene expression (Theodorakis et al 1989;Sistonen et al 1992). These observations suggest that hemin-induced RNA stabilization may be related to erythroid differentiation, physiological changes as a result of prolonged stress, or both.…”

Section: Discussionmentioning

confidence: 99%

Unraveling a cytoplasmic role for hnRNP D in the in vivo mRNA destabilization directed by the AU-rich element

Loflin¹,

Chen²,

Shyu³

1999

Genes & Development

283

256

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AU-rich RNA destabilizing elements (AREs) are found in mRNAs encoding proteins with diversified functions and synthesized under a vast variety of physiological conditions (Chen and Shyu 1995), suggesting that AREs are a key player in controlling gene expression post-transcriptionally. The potent RNA-destabilizing ability of AREs coupled with transient transcription of the corresponding genes is a prerequisite for achieving a tight temporal and spatial regulation of a transient expression of mRNA (Treisman 1985;Schiavi et al. 1992;Ross 1995). Whereas AREs are found in many different labile mRNAs, they are most commonly found in the cytokine mRNAs whose half-lives change in cells undergoing a stress response, an immune response, and responding to tissue repair (Caput et al. 1986;Shaw and Kamen 1986;Greenberg and Belasco 1993;Chen and Shyu 1995). It is now clear that the regulation of cytoplasmic mRNA turnover plays a critical role in determining the duration and level of expression of many cytokines. Recently, much has been learned concerning the key sequence features of AREs that are necessary for exerting their destabilizing function (Chen and Shyu 1995;Xu et al. 1997). Increasing reports have also been made on how alterations of certain signaling transduction pathways in lymphoid or myeloid cell lines lead to changes of the stability of cytokine mRNAs via mechanisms that require AREs, for example, IL-2, IL-3, and IL-8 mRNAs (Sirenko et al. 1997;Chen et al. 1998;Ming et al. 1998

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Section: Discussionmentioning

confidence: 99%

Unraveling a cytoplasmic role for hnRNP D in the in vivo mRNA destabilization directed by the AU-rich element

Loflin¹,

Chen²,

Shyu³

1999

Genes & Development

283

256

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“…This is well known and has been better studied in animal model systems, where some of the developmentally regulated HS genes have been identified and their transcriptional regulation analysed. The developmental regulation of HS genes depends in some cases (for example Theodorakis et al, 1989) on the same cis-acting elements as those involved in the heat shock response (HSE; reviewed by Fernandes et al, 1994a), although a functional specialization of different trans-acting factors (HSF; reviewed by Wu, 1995) that bind HSE has been described, some mammalian HSF (i.e. HSF1) being primarily involved in the heat shock response, and others (i.e.…”

Section: Introductionmentioning

confidence: 99%

Dual regulation of a heat shock promoter during embryogenesis: stage‐dependent role of heat shock elements

1998

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SummaryTransgenic tobacco expression was analysed of chimeric genes with point mutations in the heat shock element (HSE) arrays of a small heat shock protein (sHSP) gene from sunflower: Ha hsp17.7 G4. The promoter was developmentally regulated during zygotic embryogenesis and responded to heat stress in vegetative tissues. Mutations in the HSE affected nucleotides crucial for human heat shock transcription factor 1 (HSF1) binding. They abolished the heat shock response of Ha hsp17.7 G4 and produced expression changes that demonstrated dual regulation of this promoter during embryogenesis. Thus, whereas activation of the chimeric genes during early maturation stages did not require intact HSE, expression at later desiccation stages was reduced by mutations in both the proximal (-57 to -89) and distal (-99 to -121) HSE. In contrast, two point mutations in the proximal HSE that did not severely affect gene expression during zygotic embryogenesis, eliminated the heat shock response of the same chimeric gene in vegetative organs. Therefore, by site-directed mutagenesis, it was possible to separate the heat shock response of Ha hsp17.7 G4 from its developmental regulation. The results indicate the co-existence, in a single promoter, of HSF-dependent and -independent regulation mechanisms that would control sHSP gene expression at different stages during plant embryogenesis.

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“…It is found in a trimeric DNA-binding form during hemin-induced differentiation of the human erythroleukemia cells K562, in mouse embryonal carcinoma (EC) cells, and during mouse embryogenesis and spermatogenesis. During the differentiation of K562 cells, HSF2 is converted from an inert dimeric form to a DNA-binding trimer that is able to induce the transcription of Hsp70 gene [17][18][19]. In this system, it seems that although HSF1 and HSF2 are activated by distinct signals, they also induce a similar profile of heat shock gene transcription [17,18].…”

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confidence: 98%

Determination of the consensus binding sequence for the purified embryonic heat shock factor 2

Manuel¹,

Rallu²,

Loones³

et al. 2002

European Journal of Biochemistry

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Heat shock transcription factors (HSFs) are characterized by their ability, upon activation, to bind to heat shock response elements (HSE) present in the promoter of their target genes. HSE are composed of inverted repeats of the pentamer nGAAm. In this study, we compare the embryonic HSF2 protein, purified from F9 embryonal carcinoma cells tumor, and the in vitro synthesized HSF2. We show that the context of HSF2 synthesis influences its thermosensitivity and DNA-binding properties. Therefore, we determined the consensus binding sequence for the purified embryonic HSF2 by the technique of systematic evolution of ligands by exponential enrichment (SELEX). We show that embryonic HSF2 prefers sites containing three or four nGAAm inverted pentamers and that its optimal binding sequence contains the 8-mer palindromic core 5¢-TTCTAGAA-3¢. The consensus binding sequence for the embryonic HSF2 will be very helpful to identify new targets for this factor, during developmental and differentiation processes.Keywords: heat shock transcription factor-2; protein purification; cooperativity; SELEX; consensus binding sequence.Heat shock factor 2 (HSF2) belongs to the vertebrate heat shock factor family that also includes HSF1, HSF3 and HSF4 [1][2][3][4][5]. The members of the HSF family are defined by their ability to specifically bind the regulatory sequence heat shock element (HSE) [6]. Located in the regulatory regions of heat shock genes, HSE consists of the inverted repeat of a basal element nGAAm [7]. Two inverted repeats are sufficient for Drosophila HSF binding, but optimal binding is obtained with three repeats [8]. In agreement with this observation, the activated form of HSFs has been demonstrated to be a trimer in yeast [9], in Drosophila [10], in human [11,12] or in mouse [13]. The HSE-binding activity of heat shock factors is not constitutive, but induced by various stresses, by differentiation or developmental processes. HSF1 and HSF3 are activated by stresses that elicit the so-called Ôheat shock responseÕ and induce the transcription of heat shock genes. HSF1 corresponds to the paradigm member of the family and is the functional homolog, for its function in the heat shock response, of the unique HSF found in yeast and Drosophila. Avian HSF3 is activated by more severe stresses than HSF1, but is also required for an optimal response to stress [14,15]. Indeed, avian cells expressing HSF1, but in which the HSF3 gene has been disrupted, exhibit a diminished response to stress, even at mild heat shock temperatures [14]. Athough heterotrimers were never detected, HSFs may interact with each other in a more complex way.HSF4 is an exception and constitutively binds DNA as a trimer in the absence of stress. Its expression is regulated in a tissue-specific manner [5,16]. The Hsf4 gene generates both an activator or a repressor of heat shock genes by alternative splicing; the tissue-specificity of the two forms may create a modulation of expression of hsps in the different tissues.In contrast to HSF1 and HSF3, HSF2 is no...

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Hemin-induced transcriptional activation of the HSP70 gene during erythroid maturation in K562 cells is due to a heat shock factor-mediated stress response.

Cited by 88 publications

References 35 publications

Unraveling a cytoplasmic role for hnRNP D in the in vivo mRNA destabilization directed by the AU-rich element

Unraveling a cytoplasmic role for hnRNP D in the in vivo mRNA destabilization directed by the AU-rich element

Dual regulation of a heat shock promoter during embryogenesis: stage‐dependent role of heat shock elements

Determination of the consensus binding sequence for the purified embryonic heat shock factor 2

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