The plasticity of estrogen receptor–DNA complexes: Binding affinity and specificity of estrogen receptors to estrogen response element half-sites separated by variant spacers

Marzouk, Saad El; Gahattamaneni, R.; Joshi, Sachindra Raj; Scovell, William M.

doi:10.1016/j.jsbmb.2008.03.034

Cited by 27 publications

(29 citation statements)

References 53 publications

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“…The SNAP data indicated that ERE spacer sizes of 0-and 3-mer are preferred (Groups T and W; Table 2 and Fig. 5B), as has been observed previously (53). In addition, enhanced ER␣ interaction at an inverted repeat is consistent with ER␣ dimer binding, and our previous findings indicated that Pin1 enhances ER␣ dimerization (25).…”

Section: Pin1 Isomerase Function Increases Er␣ Binding Affinity To supporting

confidence: 84%

“…These findings are observed in the SSLs, in which the sequences in the central ring (perfect match to the SSL consensus; shown by arrows) of the ER␣ ϩ Pin1 landscape are of significantly higher intensity than the central ring of the ER␣-alone landscape. Comparison of the SSLs showed several Pin1-induced high intensity peaks in the outer rings, and these sequences correspond to AGGTCA direct repeats of 0 and 3 spacers, which are known ER␣ targets (53). A ridge of higher intensity peaks radiating outward in the ER␣ ϩ Pin1 landscape also contains sequences in which the motif degrades starting at the 3Ј-end.…”

Section: Regulation Of Er␣ Dna Binding Activity By Pin1mentioning

confidence: 99%

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Peptidylprolyl Isomerase Pin1 Directly Enhances the DNA Binding Functions of Estrogen Receptor α

Rajbhandari

Ozers

Solodin

et al. 2015

Journal of Biological Chemistry

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Background: Estrogen receptor ␣ (ER␣) activity in breast cancer cells is increased by Pin1, an isomerase that alters protein conformation. Results: Pin1-mediated isomerization increases ER␣ DNA binding affinity. Conclusion: Pin1 allosterically regulates ER␣ DNA binding directly via isomerization of phosphorylated receptor. Significance: Pin1 regulation of ER␣ provides a framework for understanding regulation by intrinsically disordered domains on transcription factor function.

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Section: Pin1 Isomerase Function Increases Er␣ Binding Affinity To supporting

confidence: 84%

Section: Regulation Of Er␣ Dna Binding Activity By Pin1mentioning

confidence: 99%

Peptidylprolyl Isomerase Pin1 Directly Enhances the DNA Binding Functions of Estrogen Receptor α

Rajbhandari

Ozers

Solodin

et al. 2015

Journal of Biological Chemistry

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“…For each nuclear receptor, the consensus response element has historically been defined by binding sequences usually in the form of two palindromic/inverted hexameric half sites separated by a three-nucleotide spacer, adjacent to genes transcriptionally responsive by that receptor. However, for the AR and ERa, there is evidence for interactions with sequences that do not conform to the defined consensus response element (43,44). The AR is also unique in that it can bind to response element half-sites arranged as both inverted and direct repeats (45,46).…”

Section: Discussionmentioning

confidence: 99%

Androgen Receptor Inhibits Estrogen Receptor-α Activity and Is Prognostic in Breast Cancer

et al. 2009

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There is emerging evidence that the balance between estrogen receptor-A (ERA) and androgen receptor (AR) signaling is a critical determinant of growth in the normal and malignant breast. In this study, we assessed AR status in a cohort of 215 invasive ductal breast carcinomas. AR and ERA were coexpressed in the majority (80-90%) of breast tumor cells. KaplanMeier product limit analysis and multivariate Cox regression showed that AR is an independent prognostic factor in ERApositive disease, with a low level of AR (less than median of 75% positive cells) conferring a 4.6-fold increased risk of cancer-related death (P = 0.002). Consistent with a role for AR in breast cancer outcome, AR potently inhibited ERA transactivation activity and 17B-estradiol-stimulated growth of breast cancer cells. Transfection of MDA-MB-231 breast cancer cells with either functionally impaired AR variants or the DNA-binding domain of the AR indicated that the latter is both necessary and sufficient for inhibition of ERA signaling. Consistent with molecular modeling, electrophoretic mobility shift assays showed binding of the AR to an estrogenresponsive element (ERE). Evidence for a functional interaction of the AR with an ERE in vivo was provided by chromatin immunoprecipitation data, revealing recruitment of the AR to the progesterone receptor promoter in T-47D breast cancer cells. We conclude that, by binding to a subset of EREs, the AR can prevent activation of target genes that mediate the stimulatory effects of 17B-estradiol on breast cancer cells. [Cancer Res 2009;69(15):6131-40]

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“…1). An additional motif located, at -220, is composed of two half EREs separated by a single nucleotide spacer and almost certainly does not correspond to a structural and functional ERE [5][6]32]. Compared to the consensus sequence, the two putative identified…”

Section: Putative Imperfect Ere Located In Te Sequences Within Intergmentioning

confidence: 99%

“…As pERE 2 appears as the main We next assessed the enhancer activity of this genomic region in yeast, with pY60ER and YRPE2-derivative plasmids. This convenient cellular system has long proved instrumental for the characterization of the rtER, the promoter of several E S -inducible genes and to screen the estrogenic-potency of xenobiotics [6,8,31,39]. This analysis restricted the position of the E2-dependent enhancer to a short region located between positions -130 and -190 from the TSS.…”

Section: Er Specifically Binds To the Pere2mentioning

confidence: 99%

Control of vitellogenin genes expression by sequences derived from transposable elements in rainbow trout

Bouter

Buisine

Grand

et al. 2010

Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanism

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In most of oviparous animals, vitellogenins (VTG) are the major egg yolk precursors. They are produced in the liver under the control of estrogens. In rainbow trout (Oncorhynchus mykiss), the vtg genes cluster contains an unusually large number of almost identical gene copies. In order to identify the regulatory elements in their promoters, we used a combination of reporter plasmids containing genomic sequences including putative estrogen response elements (EREs) and we performed transient transfection assays in MCF-7 and yeast cells.We found a functional ERE corresponding to the sequence GGGGCAnnnTAACCT (rtvtgERE), which differs from the consensus ERE (ERE cs ) by three base pairs. This nonpalindromic ERE is located in the env gene of a retrotransposon relic, 180 base pairs upstream of the transcriptional start site. Fluorescence anisotropy experiments confirmed that the purified human estrogen receptor α (hERα) can specifically bind to rtvtgERE. Furthermore, we observe that the stability of hERα-ERE cs and hERα-rtvtgERE complexes is similar with equilibrium dissociation constants of 3.0 nM and 6.2nM respectively, under our experimental conditions. Additionally, this rtvtgERE sequence displays a high E2-responsiveness through ER activation in cellulo.In the rainbow trout, the functional ERE (rtvtgERE) lies within promoter sequences which are mostly composed of sequences derived from transposable elements (TEs), which therefore may have acted as an evolutionary buffer to secure the proper expression of these genes.4

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The plasticity of estrogen receptor–DNA complexes: Binding affinity and specificity of estrogen receptors to estrogen response element half-sites separated by variant spacers

Cited by 27 publications

References 53 publications

Peptidylprolyl Isomerase Pin1 Directly Enhances the DNA Binding Functions of Estrogen Receptor α

Peptidylprolyl Isomerase Pin1 Directly Enhances the DNA Binding Functions of Estrogen Receptor α

Androgen Receptor Inhibits Estrogen Receptor-α Activity and Is Prognostic in Breast Cancer

Control of vitellogenin genes expression by sequences derived from transposable elements in rainbow trout

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