Prolactin upstream factor I mediates cell-specific transcription.

Cao, Zhaodan; Barron, E. A.; Sharp, Zelton Dave

doi:10.1128/mcb.8.12.5432

Cited by 26 publications

(16 citation statements)

References 29 publications

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“…A number of these sites are recognized by the pituitaryspecific POU-domain transcription factor Pit-1. The ability of Pit-1 to control prolactin gene transcription has been demonstrated repeatedly (Schuster et al 1987;Cao et al 1988;Ingraham et al 1988Ingraham et al , 1990Nelson et al 1988;Mangalam et al 1989;Elsholtz et al 1990;Fox et al 1990;Larkin et al 1990). The demonstration that Pit-1 gene dysfunction accounts for genetically dwarfed mice that fail to express the prolactin gene links Pit-1 function to transcriptional activation of the prolactin gene in the anterior pituitary (Li et al 1990).…”

mentioning

confidence: 99%

POU-domain proteins Pit-1 and Oct-1 interact to form a heteromeric complex and can cooperate to induce expression of the prolactin promoter.

Voss

Wilson²,

Rosenfeld³

1991

Genes Dev.

197

112

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mentioning

confidence: 99%

POU-domain proteins Pit-1 and Oct-1 interact to form a heteromeric complex and can cooperate to induce expression of the prolactin promoter.

Voss

Wilson²,

Rosenfeld³

1991

Genes Dev.

197

112

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“…must underlie their cell-specific and distinct temporal patterns of expression. In the case of the prolactin gene, both the promoter and a distal enhancer located 1.5 kb upstream of the transcription initiation site can confer Pit-l-dependent cell-specific activation in cell culture (Nelson et al 1986;Gutierrez-Hartman et al 1987;Cao et al 1988;Nelson et al 1988;Day and Maurer 1989;Kim et al 1989). However, the distal enhancer confers -95% of observed levels of prolactin gene expression in cell culture, and synergistic interactions between the prolactin promoter and distal enhancer region are required to achieve effective physiological levels of gene expression during normal development (Crenshaw et al 1989).…”

mentioning

confidence: 99%

Pit-1 binding to specific DNA sites as a monomer or dimer determines gene-specific use of a tyrosine-dependent synergy domain.

Holloway

Szeto²,

Scully³

et al. 1995

Genes Dev.

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Transcriptional activation of the prolactin and growth hormone genes, occurring in a cell-specific fashion, requires short-range synergistic interactions between the pituitary-specific POU domain factor Pit-1 and other transcription factors, particularly nuclear receptors. Unexpectedly, we find that these events involve the gene-specific use of alternative Pit-1 synergy domains. Synergistic activation of the prolactin gene by Pit-1 and the estrogen receptor requires a Pit-1 amino-terminal 25-amino-acid domain that is not required for analogous synergistic activation of the growth hormone promoter. The action of this Pit-1 synergy domain is dependent on the presence of two of three tyrosine residues spaced by 6 amino acids and can be replaced by a comparable tyrosine-dependent trans-activation domain of an unrelated transcription factor (hLEF). The gene-specific utilization of this tyrosine-dependent synergy domain is conferred by specific Pit-1 DNA-binding sites that determine whether Pit-1 binds as a monomer or a dimer. Thus, the critical DNA site in the prolactin enhancer, where this domain is required, binds Pit-1 as a monomer, whereas the Pit-1 sites in the growth hormone gene, which do not utilize this synergy domain, bind Pit-1 as a dimer. The finding that the sequence of specific DNA sites dictates alternative Pit-1 synergy domain utilization based on monomeric or dimeric binding suggests an additional regulatory strategy for differential target gene activation in distinct cell types.

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“…This function appears to be mediated by the cell-specific transcription factor prolactin upstream factor 1 (PUF-1) (3) (perhaps the same as Pit-1 identified previously in GC cells [14]). PUF-1, which was purified from GH3 cells, binds to a region that includes the palindrome and stimulates prolactin transcription at position +1 when it is added to nonpituitary extracts (3,4).…”

mentioning

confidence: 99%

Dual functions of a cis-acting element within the rat prolactin gene promoter.

Barron¹,

Cao²,

Schneider³

et al. 1989

Mol. Cell. Biol.

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Within the promoter region of the rat prolactin gene lies a TA-rich imperfect palindrome. The possible functions of the 18-base-pair symmetrical sequence were investigated by using an in vitro transcription system. Prolactin templates with and without the palindrome were transcriptionally assayed in both pituitary and nonpituitary extracts. Our results indicated that the palindromic sequence has at least two functions in the regulation of prolactin transcription.Enhancer elements are typically located a considerable distance from the transcriptional initiation site at position + 1 and have been shown to stimulate transcription in a tissuespecific manner in many gene systems (12,18). In addition, several recent studies have demonstrated that cis-acting elements within the proximal 5' region of some genes are also involved in cell-specific regulation (1,7,10,20). In the rat prolactin gene, an enhancer from positions -1850 to -1530 and a region of the promoter between positions -422 and -36 have been shown to augment prolactin transcription in pituitary-derived cells but not in nonpituitary-derived cells (14).Within the segment of the rat prolactin promoter from positions -422 to -36 lies an 18-base-pair (bp) imperfect palindrome, TGATTATATATATATTCA (13). Since sequences with complete or limited dyad symmetry are found frequently within regulatory elements of both procaryotic (15) and eucaryotic genes (2,8,9,11,16,17,19), it is plausible to suspect that the palindrome (positions -63 to -46) might be involved in the cell-specific regulation of prolactin transcription.This symmetrical sequence also contains five sequential TA repeats. The nucleotide composition of the palindrome is of particular interest since it constitutes a TATA homology (M. L. Goldberg, Ph.D. thesis, Stanford University, Stanford, Calif., 1979). This has raised the possibility of a second TATA element upstream of the proximal TATA box (positions -28 to -23).In the present study, the possible functions of the palindrome were investigated. Prolactin templates with and without the palindrome were assayed in pituitary-and nonpituitary-derived nuclear extracts to determine whether the palindrome is involved in the cell-specific regulation of prolactin transcription. Furthermore, since the palindrome TA repeats are homologous to the TATA consensus se- quence, the possibility of an mRNA initiation site 20 to 30 bp downstream of the palindrome was also explored.Prolactin transcription in vivo. The in vivo sites of prolactin transcriptional initiation were determined by primer extension analysis of total RNA extracted from GH3 cells (Fig. 1). These cells, which were derived from a rat pituitary tumor, constitutively produce high levels of prolactin. Approximately 10 ,ug of GH3 RNA was isolated by a modified guanidine hydrochloride procedure (5), and the RNA was assayed by primer extension analysis. An oligonucleotide primer complementary to prolactin RNA was used to detect two sites of transcriptional initiation, a major one at position + 1 and a minor RN...

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Prolactin upstream factor I mediates cell-specific transcription.

Cited by 26 publications

References 29 publications

POU-domain proteins Pit-1 and Oct-1 interact to form a heteromeric complex and can cooperate to induce expression of the prolactin promoter.

POU-domain proteins Pit-1 and Oct-1 interact to form a heteromeric complex and can cooperate to induce expression of the prolactin promoter.

Pit-1 binding to specific DNA sites as a monomer or dimer determines gene-specific use of a tyrosine-dependent synergy domain.

Dual functions of a cis-acting element within the rat prolactin gene promoter.

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