Equipotent mouse ribosomal protein promoters have a similar architecture that includes internal sequence elements.

Hariharan, Narayanan; Kelley, Dawn E.; Perry, Robert P.

doi:10.1101/gad.3.11.1789

Cited by 163 publications

(118 citation statements)

References 31 publications

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“…The various ribosomal protein genes are widely dispersed in the genome. They are transcribed at very similar rates owing to the equivalent strenghts of their promoters (Hariharan et al, 1989), and a coordinate regulation, at various levels of gene expression, operates to maintain the proper stoichiometry of the ribosomal components (Mager, 1988). In yeast, most of the ribosomal protein gene promoters contain one or two sites for a global regulator, RAP1p (Klein and Struhl 1994;Kraakman et al, 1993), and the transcription of ribosomal proteins is coordinated with rRNA synthesis (Warner, 1989).…”

Section: Ribosomal Protein and Translationally Controlled Tumor Protementioning

confidence: 99%

Differentially expressed genes in C6.9 glioma cells during vitamin D-induced cell death program

et al. 1998

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C6.9 rat glioma cells undergo a cell death program when exposed to 1,25-dihydroxyvitamin D3 (1,25-D3). As a global analytical approach, we have investigated gene expression in C6.9 engaged in this cell death program using differential screening of a rat brain cDNA library with probes derived from control and 1,25-D3-treated cells. Using this methodology we report the isolation of 61 differentially expressed cDNAs. Forty-seven cDNAs correspond to genes already characterized in rat cells or tissues. Seven cDNAs are homologous to yeast, mouse or human genes and seven are not related to known genes. Some of the characterized genes have been reported to be differentially expressed following induction of programmed cell death. These include PMP22/gas3, MGP and b-tubulin. For the first time, we also show a cell death program induced up-regulation of the c-myc associated primary response gene CRP, and of the proteasome RN3 subunit and TCTP/mortalin genes. Another interesting feature of this 1,25-D3 induced-cell death program is the down-regulated expression of transcripts for the microtubule motor dynein heavy chain/MAP 1C and of the calcium-binding S100b protein. Finally 15 upregulated cDNAs encode ribosomal proteins suggesting a possible involvement of the translational apparatus in this cell program. Alternatively, these ribosomal protein genes could be up-regulated in response to altered rates of cellular metabolism, as has been demonstrated for most of the other isolated genes which encode proteins involved in metabolic pathways. Thus, this study presents to our knowledge the first characterization of genes which are differentially expressed during a cell death program induced by 1,25-D3. Therefore, this data provides new information on the fundamental mechanisms which participate in the antineoplastic effects of 1,25-D3 and on the machinery of a cell death program in a glioma cell line.

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Section: Ribosomal Protein and Translationally Controlled Tumor Protementioning

confidence: 99%

Differentially expressed genes in C6.9 glioma cells during vitamin D-induced cell death program

et al. 1998

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“…The construction of the pL30-GH and pSl6-GH chimeras followed a similar strategy, which involved digestion of pL30CAT (construct g in ref. 36) and pS16CAT (construct c-CAT in ref. 37) *To whom reprint requests should be addressed.…”

mentioning

confidence: 99%

Oligopyrimidine tract at the 5' end of mammalian ribosomal protein mRNAs is required for their translational control.

Levy

Avni

Hariharan

et al. 1991

Proc. Natl. Acad. Sci. U.S.A.

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316

233

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Mammalian ribosomal protein (rp) mRNAs are subject to translational control, as illustrated by their selective release from polyribosomes in growth-arrested cells and their underrepresentation in polysomes in normally growing cells. In the present experiments, we have emined whether the translational control of rp mRNAs is attributable to the distinctive features of their 5' untranslated region, in particular to the oligopyrimidine tract adjacent to the cap structure. Murine lymphosarcoma cells were transfected with chimeric genes consisting of selected regions of rp mRNA fused to non-rp mRNA segments, and the translational efficiency of the resulting chimeric mRNAs was assessed in cells that either were growing normally or were growth-arrested by glucocorticoid treatment. We observed that translational control of rpL32 mRNA was abolished when its 5' untranslated region was replaced by that of .8-actin. At the same time, human growth hormone (hGH) mRNA acquired the typical behavior of rp mRNAs when it was preceded by the first 61 nucleotides of rpL30 mRNA or the first 29 nucleotides of rpS16 mRNA. Moreover, the translational control of rpSl6-hGH mRNA was abolished by the substitution of purines into the pyrimidine tract or by shortening it from eight to six residues with a concomitant cytidine -* uridine change at the 5' terminus.These results indicate that the 5'-terminal pyrimidine tract plays a critical role in the translational control mechanism. Possible factors that might interact with this translational cis regulatory element are discussed.Control at the translational level plays a dominant role in the regulated expression of eukaryotic ribosomal protein (rp) genes under a variety of conditions (1-3). These include: early development of Dictyostelium discoideum (4), Drosophila melanogaster (5)

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“…This region contains the sequence AGATGG which is common to many ribosomal protein genes (Table 1). A similar sequence in the mouse L32 gene is known to bind the zincfinger protein termed &factor or YY-1 and to enhance promoter activity [5,241. The sequence seemed repressive in this experiment, however, we can not discuss much about this region until we have directly measured the transcription activity, since the region contains a splicing donor site and translational initiation site.…”

Section: Discussionmentioning

confidence: 99%

“…Hariharan et al [5] have isolated three ribosomal protein genes from mouse and characterized their promoters. The promoters consist of several protein binding elements, some of which are common among the three genes.…”

mentioning

confidence: 99%

A Characterization of Transcriptional Regulatory Elements in Chicken Ribosomal Protein L37a Gene

Toku

Tanaka

1996

European Journal of Biochemistry

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Transcriptional control elements of chicken ribosomal protein L37a gene were characterized in terms of their activities to promote transcription and their protein binding activities. The region -120 to +168 was necessary for the maximal expression of the promoter-less CAT gene in a transfected chicken cell line. Using the DNase I protection assay, we identified nine protein binding regions distributed in a wide range of -122 to +195. The sequences of most of the elements are conserved among many vertebrate ribosomal protein genes at similar positions of the promoters. These common control elements and their binding proteins may coordinate the expression of ribosomal protein genes.

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Equipotent mouse ribosomal protein promoters have a similar architecture that includes internal sequence elements.

Cited by 163 publications

References 31 publications

Differentially expressed genes in C6.9 glioma cells during vitamin D-induced cell death program

Differentially expressed genes in C6.9 glioma cells during vitamin D-induced cell death program

Oligopyrimidine tract at the 5' end of mammalian ribosomal protein mRNAs is required for their translational control.

A Characterization of Transcriptional Regulatory Elements in Chicken Ribosomal Protein L37a Gene

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