A Gene That Is Related to <i>SRY</i> and Is Expressed in the Testes Encodes a Leucine Zipper-Containing Protein

Takamatsu, Nobuhiko; Kanda, Hiromi; Tsuchiya, Iku; Yamada, Shunji; Ito, Michihiko; Kabeno, Shoko; Shiba, Tadayoshi; Yamashita, Shinya

doi:10.1128/mcb.15.7.3759

Cited by 71 publications

(78 citation statements)

References 45 publications

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“…Using early spermatid nuclear extracts and transgenesis, a GT-rich binding region was identified in the 95-bp sequence and shown to be involved in the testis-specific expression of HSL. (8,16,24, and 48 days old) and rats (9,20,35,45, and 90 days old) were purchased from Elevage Janvier (Le Genest Saint Isle, France). Human testes were obtained from patients undergoing therapeutic orchidectomy for metastatic prostate carcinoma (protocol approved by the Ethics Committee of the city of Rennes, France).…”

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confidence: 99%

Testis Hormone-sensitive Lipase Expression in Spermatids Is Governed by a Short Promoter in Transgenic Mice

Blaise¹,

Guillaudeux²,

Tavernier³

et al. 2001

Journal of Biological Chemistry

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A testicular form of hormone-sensitive lipase (HSL tes ), a triacylglycerol lipase, and cholesterol esterase, is expressed in male germ cells. Northern blot analysis showed HSL tes mRNA expression in early spermatids. Immunolocalization of the protein in human and rodent seminiferous tubules indicated that the highest level of expression occurred in elongated spermatids. We have previously shown that 0.5 kilobase pairs of the human HSL tes promoter directs testis-specific expression of a chloramphenicol acetyltransferase reporter gene in transgenic mice and determined regions binding nuclear proteins expressed in testis but not in liver (Blaise, R., Grober, J., Rouet, P., Tavernier, G., Daegelen, D., and Langin, D. (1999) J. Biol. Chem. 274, 9327-9334). Mutation of a SRY/Sox-binding site in one of the regions did not impair in vivo testis-specific expression of the reporter gene. Further transgenic analyses established that 95 base pairs upstream of the transcription start site were sufficient for correct testis expression. In gel retardation assays using early spermatid nuclear extracts, a germ cell-specific DNA-protein interaction was mapped between ؊46 and ؊29 base pairs. The DNA binding nuclear protein showed properties of zinc finger transcription factors. Mutation of the region abolished reporter gene activity in transgenic mice, showing that it is necessary for testis expression of HSL tes . Hormone-sensitive lipase (HSL)1 hydrolyzes triacylglycerol and, cholesterol and retinyl esters (1, 2). In adipose tissue, HSL catalyzes the rate-limiting step in lipolysis, the catabolic pathway that mobilizes fatty acids from triacylglycerol stored in the lipid droplet. HSL is also expressed in rodent and human testis (3-5). In situ hybridization experiments performed in rat testis showed strong labeling of cells in the adluminal parts of the seminiferous tubules at stages X-XIV and sparsely distributed grains in the basal parts (6). Immunohistochemistry experiments showed an HSL-like immunoreactivity in the adluminal part of the rat seminiferous tubules at stages XIII-VIII (5). The data suggested that rodent HSL mRNA and protein are expressed in haploid germ cells with a lag between mRNA and protein appearance. However, the precise germ cell type(s) expressing HSL was not determined in rat and it was not possible to rule out HSL expression in Sertoli cells. Moreover, the expression of HSL in germ cells of other mammalian species, including man, has not been documented. The effects of HSL gene disruption in mice have recently been reported (7). The most striking feature of the phenotype is male sterility due to oligospermia. Degenerated spermatocytes and spermatids were observed in HSL-deficient testis with a lack of mature spermatozoa. The data clearly demonstrate that HSL is required for spermatogenesis.The human adipose tissue form of HSL is encoded by 9 exons spanning 11 kb (8). The transcription start site was mapped in a short 5Ј-noncoding exon located 1.5 kb upstream of the first coding exon (9). The 2.8-kb mR...

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confidence: 99%

Testis Hormone-sensitive Lipase Expression in Spermatids Is Governed by a Short Promoter in Transgenic Mice

Blaise¹,

Guillaudeux²,

Tavernier³

et al. 2001

Journal of Biological Chemistry

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“…The activation is facilitated by the dimerization of the long form of SOX5 and SOX6. SOX6 contains a leucine zipper motif that allows dimerization of the protein, and homodimers fail to bind DNA (40). These data suggest that, in testis, SOX6 may bind to another protein as a heterodimer to show transactivation properties.…”

Section: Discussionmentioning

confidence: 81%

Mouse μ Opioid Receptor Distal Promoter Transcriptional Regulation by SOX Proteins

Hwang

Wang

et al. 2003

Journal of Biological Chemistry

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We have identified transcription factors that bind to specific sequences in 5 -distal promoter regulatory sequences of the mouse opioid receptor (mor) promoter using the yeast one-hybrid system. The sequence between ؊746 and ؊707 in mor distal promoter was used as the bait because it acts as a functional promoter element and binds several DNA-binding proteins. From an adult mouse brain cDNA library, five cDNA clones encoding three Sox gene family (Sry like high mobility group (HMG) box gene) transcriptional factors, mSOX18, mSOX21, and mSOX6, were isolated. Electrophoretic mobility shift assays confirmed the presence of a binding site for SOX proteins in the ؊731/؊725 region. Additionally, we have also established that the flanking regions outside the core Sox-binding site play an essential role in high affinity binding. DNase I footprint analysis indicates that proteins from mouse brain interact with the Sox-binding site within the mor distal promoter. Finally, we demonstrated that overexpression of mSOX18 and/or mSOX21 was able to up-regulate mouse mor distal promoter activity in mor-expressing neuronal cells (NMB). These data indicate that SOX proteins might contribute to the transcriptional activity of the mor gene and suggest that opioid receptor could mediate some of the developmental processes in which SOX proteins are included.Opioids have many pharmacological and physiological effects, including analgesia, sedation, euphoria, and respiratory depression and also induce tolerance and physical dependence when administered chronically. Pharmacological, physiological, receptor binding, and molecular cloning studies (1) have revealed that opioids interact with three major types of opioid receptors in the mammalian central nervous system and peripheral tissues, , ␦, and . All three types of receptors belong to the superfamily of G-protein-coupled receptors (2), and the opioid receptor (mor) 1 is known to play the essential role in morphine-induced analgesia, tolerance, and dependence as indicated from pharmacological studies. This has also been confirmed by additional in vivo pharmacological analyses of mice where mor was deleted by homologous recombination (3).Mor is expressed mainly in the central nervous system, where it exhibits distinct temporal and spatial patterns of distribution (1). Recently, in situ hybridization studies and other methods (e.g. RPA (RNase protection assay) and reverse transcriptase-PCR) indicate that expression of mor mRNA is regulated at the transcriptional level, especially during embryonic development (4 -7). The molecular mechanisms underlying this regulation are not completely understood, but analysis of the 5Ј-upstream sequences from the translation initiation sites of the mor gene has shown that expression of mor is driven by two promoters, a distal and a proximal promoter (8). Both promoters exhibit characteristics of housekeeping genes lacking a TATA box (9, 10), with the proximal promoter regulating mor transcription from four major initiation sites located in a region 291-...

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“…Using the soluble fraction of the E. coli lysate which contained the recombinant protein, gel retardation analysis was performed as described previously [14]. The sequences of duplex oligonucleotide probes are as follows: Mut-ll, 5'-GGGAGAGAACAATGGGTGCCCTAC-3'; HuSRY, 5'-GGGGTTAACGTAACAAAGAATCTGGTAGA-3'; HuAllmut, 5'-GGGGTTAACGTCCGCGGTAATCTGGTAGA-3'.…”

Section: Gel Retardation Analysismentioning

confidence: 99%

“…The sequences of duplex oligonucleotide probes are as follows: Mut-ll, 5'-GGGAGAGAACAATGGGTGCCCTAC-3'; HuSRY, 5'-GGGGTTAACGTAACAAAGAATCTGGTAGA-3'; HuAllmut, 5'-GGGGTTAACGTCCGCGGTAATCTGGTAGA-3'. The oligonucleotides were labeled with [c~-32p]dCTP by Klenow fragment described previously [14]. …”

Section: Gel Retardation Analysismentioning

confidence: 99%

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A rainbow trout SRY‐type gene expressed in pituitary glands

et al. 1995

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A Sox (SRY-type HMG box) gene, designated SoxP1, was isolated from a cDNA library made from pituitaries of immature rainbow trout. Sequence analysis indicated that the cDNA had an open reading frame encoding 467 amino acid residues containing a DNA binding motif, known as the high mobility group (HMG) box. Northern blot analysis showed trout SoxP1 mRNA was detected in pituitaries and gonadal tissues, but not in liver, spleen, and heart. In pituitaries, trout SoxP1 mRNA was more abundant in immature fish than in mature fish. Gel shift retardation analysis indicated that the recombinant HMG box protein of SoxP1 produced in E. coli had a DNA binding property for an AACAAT or AACAAAG sequence. These findings suggest that the trout SoxP1 protein may play certain roles in growth or maturation in pituitaries as a transcription factor.

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A Gene That Is Related to SRY and Is Expressed in the Testes Encodes a Leucine Zipper-Containing Protein

Cited by 71 publications

References 45 publications

Testis Hormone-sensitive Lipase Expression in Spermatids Is Governed by a Short Promoter in Transgenic Mice

Testis Hormone-sensitive Lipase Expression in Spermatids Is Governed by a Short Promoter in Transgenic Mice

Mouse μ Opioid Receptor Distal Promoter Transcriptional Regulation by SOX Proteins

A rainbow trout SRY‐type gene expressed in pituitary glands

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