An everted repeat mediates retinoic acid induction of the gamma F-crystallin gene: evidence of a direct role for retinoids in lens development.

Tini, Mark; Otulakowski, Gail; Breitman, Martin L.; Tsui, Lap‐Chee; Giguère, Vincent

doi:10.1101/gad.7.2.295

Cited by 156 publications

(80 citation statements)

References 73 publications

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“…Cell culture experiments identified two enhancer-like regions, -392/-278 and −226/-121; however, they were never tested in transgenic mice (Yu et al, 1990). Transcription factor binding sites for Pax6 (Kralova et al, 2002), RARβ/RXRβ (Tini et al, 1993) Six3, Prox1 ), Hsf4 (Fujimoto et al, 2004), Sox1 and Sox2 (Kamachi et al, 1995), large Mafs (Rajaram and Kerppola, 2004) and TFIID were identified within the −226 to +45 fragment (see Fig. 13).…”

Section: 23mentioning

confidence: 99%

Genetic and epigenetic mechanisms of gene regulation during lens development

Cvekl

Duncan

2007

Progress in Retinal and Eye Research

137

122

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Recent studies demonstrated a number of links between chromatin structure, gene expression, extracellular signaling and cellular differentiation during lens development. Lens progenitor cells originate from a pool of common progenitor cells, the pre-placodal region (PPR) which is formed due to a complex exchange of extracellular signals between the neural plate, naïve ectoderm and mesendoderm. A specific commitment to the lens program over alternate choices such as the formation of olfactory epithelium or the anterior pituitary is manifested by the formation of a thickened surface ectoderm, the lens placode. Mouse lens progenitor cells are characterized by the expression of a complement of lens lineage-specific transcription factors including Pax6, Six3 and Sox2, controlled by FGF and BMP signaling, followed later by c-Maf, Mab21like1, Prox1 and FoxE3. Proliferation of lens progenitors together with their morphogenetic movements results in the formation of the lens vesicle. This transient structure, comprised of lens precursor cells, is polarized with its anterior cells retaining their epithelial morphology and proliferative capacity, whereas the posterior lens precursor cells initiate terminal differentiation forming the primary lens fibers. Lens differentiation is marked by expression and accumulation of crystallins and other structural proteins. The transcriptional control of crystallin genes is characterized by the reiterative use of transcription factors required for the establishment of lens precursors in combination with more ubiquitously expressed factors (e.g. AP-1, AP-2α, CREB and USF) and recruitment of histone acetyltransferases (HATs) CBP and p300, and chromatin remodeling complexes SWI/SNF and ISWI. These studies have poised the study of lens development at the forefront of efforts to understand the connections between development, cell signaling, gene transcription and chromatin remodeling.

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Section: 23mentioning

confidence: 99%

Genetic and epigenetic mechanisms of gene regulation during lens development

Cvekl

Duncan

2007

Progress in Retinal and Eye Research

137

122

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“…Cold Spring Harbor Laboratory Press on May 12, 2018 -Published by genesdev.cshlp.org Downloaded from together determine the affinity and specificity of interactions between RARs, TRs, and VDRs and their respective response element sequences in target genes Baniahmad et al 1990;Lazar et al 1991;Niiiir et al 1991;Umesono et al 1991;Forman et al 1992;Carlberg et al 1993;Tini et al 1993). The studies presented in this paper indicate that the association of the TR, VDR, and RAR with RXR results in their preferential recognition of direct repeat elements.…”

Section: Preferential Recognition Of Direct Repeat Elements By Rxr Hementioning

confidence: 99%

“…First, in contrast to the estrogen and glucocorticoid receptors, which appear to bind to DNA exclusively as homodimers, the TRs or RARs preferentially interact with their cognate response elements as components of heterodimeric complexes containing retinoid X receptors (RXRs} [Yu et al 19911 Kliewer et al 1992~ Leid et al 19921 Marks et al 1992~ Zhang et al 1992 and perhaps other nuclear proteins [Murray andTowle 19891 Burnside et al 1990~ Glass et al 19901 Liao et al 1990). Second, whereas steroid hormone receptors preferentially bind to response elements consisting of a palindromic arrangement of a conserved recognition motif, heterodimers of the TR or RAR complexed with the RXR bind with high affinity and activate transcription from response elements consisting of direct repeat, palindromic, and inverted palindromic arrangements of a core recognition motif of the consensus sequence AGGTCA Umesono et al 1988Umesono et al , 1991Baniahmad et al 1990;Carlberg et al 1993;Tini et al 1993).…”

mentioning

confidence: 99%

Differential orientations of the DNA-binding domain and carboxy-terminal dimerization interface regulate binding site selection by nuclear receptor heterodimers.

Kurokawa¹,

Yu²,

Näär³

et al. 1993

Genes & Development

346

194

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Retinoic acid, thyroid hormone, and vitamin D receptors preferentially activate target genes through response elements that consist of direct repeat arrangements of a core recognition motif of consensus sequence AGGTCA. We present evidence that the preference for direct repeat elements arises from two fundamental differences from steroid hormone receptors. First, retinoic acid, thyroid hormone, and vitamin D receptors are demonstrated to preferentially form heterodimers with the retinoid X receptors. These interactions are mediated by the carboxy-terminal dimerization interface, with heterodimer preference specified by actions of the DNA-binding domain. Second, the DNA-binding domains of heterodimeric receptors appear to be rotationally flexible with respect to the carboxy-terminal dimerization interface. Several independent lines of evidence suggest that, relative to the retinoid X and steroid hormone receptors, the DNA-binding domain of the thyroid hormone receptor is preferentially rotated by -180 ~ with respect to its carboxy-terminal dimerization interface. As a result, solution interactions between the carboxy-terminal dimerization interfaces of the retinoid X and thyroid hormone receptors are predicted to lead to the preferential alignment of their respective DNA-binding domains in a direct repeat configuration. This alignment would position the retinoid X receptor over the upstream recognition motif of direct repeat response elements. Differential orientations of the DNA-binding domain, which contribute to the polarity of heterodimer binding, are regulated by a short sequence (the A box) that is located between the conserved DNA-binding and carboxy-terminal dimerization domains.[Key Words: Nuclear receptor heterodimersl DNA-binding domain~ carboxy-terminal dimerization interface] Received April 9, 1993~ revised version accepted May 13, 1993.The thyroid hormone, retinoic acid, and vitamin D receptors [TR, RAR, and VDR, respectively} are members of the nuclear receptor superfamily of ligand-dependent transcription factors that interact with response elements in target genes and thereby control diverse aspects of development and homeostasis (Evans 1988~ Beato 1989~ Glass and Rosenfeld 1991}. A central problem in understanding the actions of these and related nuclear receptors is the elucidation of the molecular mechanisms by which target genes are recognized. Studies of the DNA-binding properties of the TR, RAR, and VDR SCorgesponding author. 6Present address:

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“…Other potential candidates include members of the nuclear receptor superfamily, which may bind large elements that have a palindromic structure. In this respect, the Pal elements most closely resemble a thyroid-hormone-response element which is found in the promoter region of the γF-crystallin gene and is an everted repeat [27,28]. However, since members of this superfamily are typically less than 50 M r in size, it seems unlikely that they bind to the Pal elements.…”

Section: Discussionmentioning

confidence: 99%

The Pal elements in the upstream glucokinase promoter exhibit dyad symmetry and display cell-specific enhancer activity when multimerised

Moates

Magnuson

2004

Diabetologia

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Aims/hypothesis. The upstream glucokinase (βGK) promoter has previously been shown to contain two 9-bp sequences, termed the Pal motifs, that are conserved in humans, rats and mice. These motifs are necessary for expression of the βGK promoter in pancreatic beta cell lines and pituitary corticotrope cell lines. DNA probes containing the Pal motifs bind celltype-specific protein complexes, but these motifs have not been completely characterised. Methods. Methylation interference and ultravioletcrosslinking analysis were utilised to characterise, at the single nucleotide level, sites of protein binding within the elements themselves. To determine the function of these elements, mutational analysis of the βGK promoter and of multimerised GK promoter sequences was performed.Results. Both Pal elements are 14 bp in length and have dyad symmetry. However, while the Pal-1 element is a perfect inverted repeat (GTCACCA-TGGT-GAC), the Pal-2 element (GTCACCA-TAGAAAC) is an imperfect repeat. Ultraviolet-crosslinking analysis using nuclear extracts prepared from hamster insulinoma tumour (HIT) cells revealed that the three resolvable complexes that bind to the Pal-1 and Pal-2 elements contain different ratios of three proteins of different size (~90, 110 and 150 M r ). Mutation of a single nucleotide binding site abrogates βGK promoter activity. Multimerised repeats of the Pal-1 element augment transcription in HIT cells, but not in baby hamster kidney (BHK) cells. Conclusions/interpretation. These results suggest that different combinations of three proteins of different size bind to the Pal elements, probably as homodimers and heterodimers. Together, these results indicate that the βGK promoter contains two novel 14-bp elements that, when multimerised, exhibit enhancer activity specific to neuroendocrine cells.

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An everted repeat mediates retinoic acid induction of the gamma F-crystallin gene: evidence of a direct role for retinoids in lens development.

Cited by 156 publications

References 73 publications

Genetic and epigenetic mechanisms of gene regulation during lens development

Genetic and epigenetic mechanisms of gene regulation during lens development

Differential orientations of the DNA-binding domain and carboxy-terminal dimerization interface regulate binding site selection by nuclear receptor heterodimers.

The Pal elements in the upstream glucokinase promoter exhibit dyad symmetry and display cell-specific enhancer activity when multimerised

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