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Transcription (biology)

About: Transcription (biology) is a research topic. Over the lifetime, 56532 publications have been published within this topic receiving 2952782 citations. The topic is also known as: genetic transcription & transcription, genetic.


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Journal ArticleDOI
10 Mar 1971-Nature
TL;DR: This work has made use of the observation that free ribosomes from hamster cells form dimers in conditions where mouse free Ribosomes remain as monomers, dimers or as both to determine whether mouse-hamster hybrid cells contain freeribosomes as monomer, dimer or both.
Abstract: ONLY mouse 28S ribosomal RNA (rRNA) can be detected in mouse-human hybrid cells1. Because these cells contain as many as thirty-five human chromosomes, including those believed to have ribosomal RNA genes, it has been suggested that the transcription of human ribosomal RNA genes may be repressed. Similar studies have not been performed with mouse-hamster hybrid cells because hamster and mouse 28S rRNAs have only a very small difference in their electro-phoretic mobilities2. We have now made use of the observation that free ribosomes (not engaged in translation) from hamster cells form dimers in conditions where mouse free ribosomes remain as monomers3 to determine whether mouse-hamster hybrid cells contain free ribosomes as monomers, dimers or as both.

539 citations

Journal ArticleDOI
Ryohei Yagi1, Lin Feng Chen1, Katsuya Shigesada1, Yota Murakami1, Yoshiaki Ito1 
TL;DR: It is shown here that mutation of the PY motif in the subregion of the activation domain of the DNA‐binding subunit of PEBP 2, PEBP2α, abolishes its transactivation function.
Abstract: A protein module called the WW domain recognizes and binds to a short oligopeptide called the PY motif, PPxY, to mediate protein-protein interactions. The PY motif is present in the transcription activation domains of a wide range of transcription factors including c-Jun, AP-2, NF-E2, C/EBPalpha and PEBP2/CBF, suggesting that it plays an important role in transcriptional activation. We show here that mutation of the PY motif in the subregion of the activation domain of the DNA-binding subunit of PEBP2, PEBP2alpha, abolishes its transactivation function. Using yeast two-hybrid screening, we demonstrate that Yes-associated protein (YAP) binds to the PY motif of PEBP2alpha through its WW domain. The C-terminal region of YAP fused to the DNA-binding domain of GAL4 showed transactivation as strong as that of GAL4-VP16. Exogenously expressed YAP conferred transcription-stimulating activity on the PY motif fused to the GAL4 DNA-binding domain as well as to native PEBP2alpha. The osteocalcin promoter was stimulated by exogenous PEBP2alphaA and a dominant negative form of YAP strongly inhibited this activity, suggesting YAP involvement in this promoter activity in vivo. These results indicate that the PY motif is a novel transcription activation domain that functions by recruiting YAP as a strong transcription activator to target genes.

538 citations

Journal ArticleDOI
TL;DR: Nrf2 appears to autoregulate its own expression through an ARE-like element located in the proximal region of its promoter, leading to persistent nuclear accumulation of Nrf2 and protracted induction of phase 2 genes in response to chemopreventive agents.
Abstract: Induction of phase 2 enzymes, which neutralize reactive electrophiles and act as indirect antioxidants, is an important mechanism for protection against carcinogenesis. The transcription factor Nrf2, which binds to the antioxidant response element (ARE) found in the upstream regulatory region of many phase 2 genes, is essential for the induction of these enzymes. We have investigated the effect of the potent enzyme inducer and anticarcinogen 3H-1,2-dithiole-3-thione (D3T) on the fate of Nrf2 in murine keratinocytes. Both total and nuclear Nrf2 levels increased rapidly and persistently after treatment with D3T but could be blocked by cotreatment with cycloheximide. Nrf2 mRNA levels increased approximately 2-fold 6 h after D3T treatment. To examine the transcriptional activation of Nrf2 by D3T, the proximal region (1 kb) of the nrf2 promoter was isolated. Deletion and mutagenesis analyses demonstrated that nrf2 promoter-luciferase reporter activity was enhanced by treatment with D3T and that ARE-like sequences were required for this activation. Gel shift assays with nuclear extracts from PE cells indicated that common factors bind to typical AREs and the ARE-like sequences of the nrf2 promoter. Direct binding of Nrf2 to its own promoter was demonstrated by chromatin immunoprecipitation assay. Overexpression of Nrf2 increased the activity of the nrf2 promoter-luciferase reporter, while expression of mutant Nrf2 protein repressed activity. Thus, Nrf2 appears to autoregulate its own expression through an ARE-like element located in the proximal region of its promoter, leading to persistent nuclear accumulation of Nrf2 and protracted induction of phase 2 genes in response to chemopreventive agents.

538 citations

Journal ArticleDOI
29 Jul 1988-Cell
TL;DR: These results establish a key role for fos in signal transduction and implicate the fos protein as a trans-activating and -repressing molecule.

537 citations

Journal ArticleDOI
TL;DR: Transfection of cDNA clones into Drosophila cells indicates that the AP-2 gene product can also activate gene expression in vivo in a DNA template-dependent manner and may be a transcription factor involved in the control of developmentally regulated gene expression.
Abstract: Human AP-2 is a sequence-specific DNA-binding protein that interacts with inducible viral and cellular enhancer elements to stimulate transcription of selected genes. Here, we report the isolation and characterization of a human cDNA clone containing the entire protein-coding region of AP-2. The deduced primary amino acid sequence of AP-2 does not contain a domain resembling any previously identified DNA binding motif. However, an interesting feature of the AP-2 protein is a clustered arrangement of proline and glutamine residues that have been found recently within the activation domains of other transcription factors. Expression of the AP-2 clone in bacteria yields a protein that binds to DNA and activates transcription in vitro in a comparable manner to native human AP-2. Transfection of cDNA clones into Drosophila cells indicates that the AP-2 gene product can also activate gene expression in vivo in a DNA template-dependent manner. Expression of endogenous AP-2 is repressed in a hepatoma cell line and stimulated following retinoic-acid-induced differentiation of a human teratocarcinoma cell line. This indicates that AP-2 may be a transcription factor involved in the control of developmentally regulated gene expression.

536 citations


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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
20229
20211,730
20201,721
20191,686
20181,571
20171,465