The p100 EBNA-2 coactivator: a highly conserved protein found in a range of exocrine and endocrine cells and tissues in cattle
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 de...
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description | 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. |
doi_str_mv | 10.1016/j.bbaexp.2004.10.009 |
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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.</description><identifier>ISSN: 0167-4781</identifier><identifier>ISSN: 0006-3002</identifier><identifier>EISSN: 1879-2634</identifier><identifier>DOI: 10.1016/j.bbaexp.2004.10.009</identifier><identifier>PMID: 15627504</identifier><language>eng</language><publisher>Netherlands: Elsevier B.V</publisher><subject>4SNc-tudor ; Amino Acid Sequence ; Animals ; Base Sequence ; Blotting, Northern ; Blotting, Western ; Cattle ; DNA, Complementary ; Endocrine Glands - metabolism ; Evolution, Molecular ; Exocrine Glands - metabolism ; Humans ; Immunohistochemistry ; Mammary ; Mice ; Nuclear Proteins - genetics ; Nuclear Proteins - metabolism ; Nuclease ; Pancreas ; Phylogeny ; RNA, Messenger - metabolism ; Tudor domain</subject><ispartof>Biochimica et biophysica acta, 2005-01, Vol.1681 (2), p.126-133</ispartof><rights>2004 Elsevier B.V.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c457t-8e9d1548a553d3d1424a21aeea723b7ca001da566ef067b38c768cd816e012f23</citedby><cites>FETCH-LOGICAL-c457t-8e9d1548a553d3d1424a21aeea723b7ca001da566ef067b38c768cd816e012f23</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15627504$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Broadhurst, Marita K.</creatorcontrib><creatorcontrib>Lee, Rita S.-F.</creatorcontrib><creatorcontrib>Hawkins, Sarah</creatorcontrib><creatorcontrib>Wheeler, Thomas T.</creatorcontrib><title>The p100 EBNA-2 coactivator: a highly conserved protein found in a range of exocrine and endocrine cells and tissues in cattle</title><title>Biochimica et biophysica acta</title><addtitle>Biochim Biophys Acta</addtitle><description>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.</description><subject>4SNc-tudor</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>Blotting, Northern</subject><subject>Blotting, Western</subject><subject>Cattle</subject><subject>DNA, Complementary</subject><subject>Endocrine Glands - metabolism</subject><subject>Evolution, Molecular</subject><subject>Exocrine Glands - metabolism</subject><subject>Humans</subject><subject>Immunohistochemistry</subject><subject>Mammary</subject><subject>Mice</subject><subject>Nuclear Proteins - genetics</subject><subject>Nuclear Proteins - metabolism</subject><subject>Nuclease</subject><subject>Pancreas</subject><subject>Phylogeny</subject><subject>RNA, Messenger - metabolism</subject><subject>Tudor domain</subject><issn>0167-4781</issn><issn>0006-3002</issn><issn>1879-2634</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFUUFvFCEYJUZjt9V_YAwnb7PyAQOzHkxq06pJ017qmTDwTZfN7LACu2kv_nYZdxNvygW-x3uPFx4h74AtgYH6uFn2vcWn3ZIzJiu0ZGz1giyg06uGKyFfkkWl6UbqDs7Iec4bVpcC9ZqcQau4bplckF8Pa6Q7YIxef7m7bDh10boSDrbE9Ilaug6P6_G5olPGdEBPdykWDBMd4n7ytB4sTXZ6RBoHik_RpTAhtfUKJ3-aHI5j_oOVkPMe8yxztpQR35BXgx0zvj3tF-THzfXD1bfm9v7r96vL28bJVpemw5WHVna2bYUXHiSXloNFtJqLXjvLGHjbKoUDU7oXndOqc74DhQz4wMUF-XD0rfF_1gTFbEOec9kJ4z4bpYUQrIX_EkFXZw6zozwSXYo5JxzMLoWtTc8GmJkLMhtzLMjMBc1oLajK3p_89_0W_V_RqZFK-HwkYP2OQ8Bksgs4OfQhoSvGx_DvF34Df0WinQ</recordid><startdate>20050111</startdate><enddate>20050111</enddate><creator>Broadhurst, Marita K.</creator><creator>Lee, Rita S.-F.</creator><creator>Hawkins, Sarah</creator><creator>Wheeler, Thomas T.</creator><general>Elsevier B.V</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7TM</scope><scope>7X8</scope></search><sort><creationdate>20050111</creationdate><title>The p100 EBNA-2 coactivator: a highly conserved protein found in a range of exocrine and endocrine cells and tissues in cattle</title><author>Broadhurst, Marita K. ; Lee, Rita S.-F. ; Hawkins, Sarah ; Wheeler, Thomas T.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c457t-8e9d1548a553d3d1424a21aeea723b7ca001da566ef067b38c768cd816e012f23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>4SNc-tudor</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Base Sequence</topic><topic>Blotting, Northern</topic><topic>Blotting, Western</topic><topic>Cattle</topic><topic>DNA, Complementary</topic><topic>Endocrine Glands - metabolism</topic><topic>Evolution, Molecular</topic><topic>Exocrine Glands - metabolism</topic><topic>Humans</topic><topic>Immunohistochemistry</topic><topic>Mammary</topic><topic>Mice</topic><topic>Nuclear Proteins - genetics</topic><topic>Nuclear Proteins - metabolism</topic><topic>Nuclease</topic><topic>Pancreas</topic><topic>Phylogeny</topic><topic>RNA, Messenger - metabolism</topic><topic>Tudor domain</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Broadhurst, Marita K.</creatorcontrib><creatorcontrib>Lee, Rita S.-F.</creatorcontrib><creatorcontrib>Hawkins, Sarah</creatorcontrib><creatorcontrib>Wheeler, Thomas T.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Nucleic Acids Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Biochimica et biophysica acta</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Broadhurst, Marita K.</au><au>Lee, Rita S.-F.</au><au>Hawkins, Sarah</au><au>Wheeler, Thomas T.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The p100 EBNA-2 coactivator: a highly conserved protein found in a range of exocrine and endocrine cells and tissues in cattle</atitle><jtitle>Biochimica et biophysica acta</jtitle><addtitle>Biochim Biophys Acta</addtitle><date>2005-01-11</date><risdate>2005</risdate><volume>1681</volume><issue>2</issue><spage>126</spage><epage>133</epage><pages>126-133</pages><issn>0167-4781</issn><issn>0006-3002</issn><eissn>1879-2634</eissn><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.</abstract><cop>Netherlands</cop><pub>Elsevier B.V</pub><pmid>15627504</pmid><doi>10.1016/j.bbaexp.2004.10.009</doi><tpages>8</tpages></addata></record> |
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subjects | 4SNc-tudor Amino Acid Sequence Animals Base Sequence Blotting, Northern Blotting, Western Cattle DNA, Complementary Endocrine Glands - metabolism Evolution, Molecular Exocrine Glands - metabolism Humans Immunohistochemistry Mammary Mice Nuclear Proteins - genetics Nuclear Proteins - metabolism Nuclease Pancreas Phylogeny RNA, Messenger - metabolism Tudor domain |
title | The p100 EBNA-2 coactivator: a highly conserved protein found in a range of exocrine and endocrine cells and tissues in cattle |
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