Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
9885598 | Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression | 2005 | 8 Pages |
Abstract
The p100 transcriptional coactivator is an evolutionarily conserved protein that has been shown to be a coactivator of the Epstein-Barr virus-encoded transcription factor EBNA-2, as well as Stat5 and Stat6. However, the p100 genomic organisation, phylogeny and expression have not been analysed in detail and its physiological role is uncertain. The cDNA and amino acid sequence of bovine p100 was obtained, and the genomic organisation of the human p100 gene was determined. Homologues of p100 were found in the genomes of 21 diverse eukaryotes. Western blot and immunohistochemical analyses revealed that the bovine p100 protein is present in a range of exocrine and endocrine cells and tissues, including the lactating mammary gland, pancreas, adrenal, parotid, anterior pituitary, corpus luteum, ovarian follicular cells, placenta and small intestine. P100 was present in the nuclei of mammary epithelial cells and pancreatic acinar cells, but only in the extranuclear compartment of the other immunopositive tissues. These data indicate that the p100 protein plays a fundamental role in eukaryotic biology, and functions in secretory cells, at least in cattle.
Keywords
UTREBNA-2ORFRT-PCRIPTGcDNADNA complementary to RNAPSI-BLASTamino acidPosition-Specific Iterated BLASTBlastisopropyl β-D-1-thiogalactopyranosideNucleaserapid amplification of cDNA endsTudor domainopen reading frameRaceuntranslated regionNucleotidepolymerase chain reactionreverse transcription polymerase chain reactionPCRPancreasMammary
Related Topics
Life Sciences
Biochemistry, Genetics and Molecular Biology
Biochemistry
Authors
Marita K. Broadhurst, Rita S.-F. Lee, Sarah Hawkins, Thomas T. Wheeler,