RET/PTC activation in human thyroid carcinomas.
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Animals↗
Biomedical subjects
N Dathan
Publications and source records attributed to N Dathan.
Delineation of human papillomavirus type 18 enhancer binding proteins: the intracellular distribution of a novel octamer binding protein p92 is cell cycle regulated.
The enhancer of human papillomavirus type 18 consists of two functionally redundant domains, one is partially conserved between HPV18 and HPV16, both mediate strong transcriptional enhancement. In contrast, short fragments of the enhancer mediate low transcriptional enhancement, suggesting that there is functional cooperation between HPV enhancer binding factors. Previously interactions of the enhancer with NF-1, AP1 and steroid receptors were shown by EMSA. Here we show by binding site blotting, that four novel sequence specific proteins p110, p92, p42 and p40 bind to the enhancer. Nuclear proteins p110 and p92 bind at repeated sites in the enhancer, proteins p42 and p40 only at one site. Recognition sequences for p110 and p92 were identified in a TTGCTTGCATAA sequence motif and consist of an overlapping p110 and p92 recognition site. The specific interaction of p110 with G residues of this 12 nucleotide long sequence was demonstrated by a mutant recognition site. Single recognition sites for p42 and p40 were localized in the enhancer by the use of overlapping oligonucleotides. In addition, electrophoretic mobility shift analysis identified Oct-1 and AP2 interactions with the enhancer. The AP2 binding site was mapped to a AGGCACATATT motif. The p92 protein binds to enhancer oligonucleotides, containing at least one copy of Oct-1 like recognition sequences, these oligonucleotides also bind synthetic Oct-1 protein. During serum starvation or at high saturation density, p92 moves from the nucleus into the cytoplasm. Immunoblots of cytoplasmic extracts with anti-Oct-1 antisera showed, that p92 is a novel octamer binding factor, which is not immunologically related to the Oct-1 protein. The intracellular p92 distribution is regulated at the G0/G1 boundary of the cell cycle, by nucleo-cytoplasmic translocation.
Base Sequence↗
Xenopus myc proto-oncogene during development: expression as a stable maternal mRNA uncoupled from cell division.
A Xenopus cDNA clone highly homologous to the proto-oncogene c-myc has been isolated and used to derive a homologous probe to study myc expression during embryonic development. Myc RNA is identified as a member of the class of maternal mRNAs expressed before fertilisation. It is highly accumulated from early oogenesis and an unfertilised egg contains 8 pg, about 10(5)-fold the myc content of proliferative somatic cells. After fertilisation a post-transcriptional regulation of the gene is induced and the accumulated myc RNA is degraded (t1/2 = 4 h 20 min) to reach a level at gastrula of 10 transcripts per cell; a value maintained during subsequent embryonic development. The Xenopus myc protein has also been identified by both myc-specific antibodies and hybrid selection experiments. Translation in vitro of Xenopus myc RNA shows that it encodes a 62-kd protein which is also recognised by myc antibodies in oocyte extracts. This protein is accumulated in late oogenesis. The results indicate an unusual uncoupling of myc expression and cell proliferation linked to a stabilisation of the RNA product.
Animals↗
Formation of the 3' end on U snRNAs requires at least three sequence elements.
The structural requirements for 3' end formation on the Xenopus laevis U1B snRNA gene have been studied. Three sequence elements are shown to be required. The first is a conserved sequence element found immediately 3' of all vertebrate U snRNA genes studied so far. The second is a gene internal sequence potentially capable of forming a stem-loop structure close to the 3' end of the RNA. The third element lies upstream of these, and may be part of the gene promoter. Experiments designed to investigate the mechanism of 3' end formation on primary U1B snRNA transcripts failed to find evidence for a processing event.
Acetyltransferases↗
Cell type-specific activation of actin genes in the early amphibian embryo.
Muscle actin genes are the earliest yet described to show cell type-specific activation in amphibian embryos. Gene-specific probes show that alpha-skeletal and alpha-cardiac actin genes start to be transcribed simultaneously at the end of gastrulation, but only in those regions of the mesoderm that subsequently form embryonic muscle. Their expression provides a molecular marker for early cell determination.
Actins↗