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Title[redir]:
Hepatitis B Virus X-Associated Protein 2 Is a Subunit of the Unliganded Aryl Hydrocarbon Receptor Core Complex and Exhibits Transcriptional Enhancer Activity: Molecular and Cellular Biology: Vol 18 , No 2 - Get Access
Description:
The aryl hydrocarbon receptor (AhR) is a ligand-inducible transcription factor that is a member of the bHLH-PAS (basic helix-loop-helix Per-Arnt-Sim) regulatory protein superfamily and is central i...
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access, journals, sciences, open, taylor, francis, search, article, science, online, journal, studies, xap, browse, log, molecular, university, ahr, find, environment, protein, articles, group, page, publish, health, social, information, cart, issue, complex, pennsylvania, fkbp, pdf, technology, register, read, content, close, menu, select, calls, papers, suggester, publishing, guidance, author, services, bioscience, earth,
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social care medicine journals bioscience molecular downloaded article pdf twitter page taylor article /doi/full/10 veterinary science francis group ahr ligand-binding subunit journal search calls cart search downloaded article pdfs unliganded ahr complex limited period read lists articles find guidance advanced search molecular institution access published online journals books 330-amino-acid protein receive personalised research crossref citations citing articles based journals browse author services home meyera graduate program perdewa graduate program carboxy-terminal region polyclonal antibodies raised keck biopolymer facility gel tryptic digestions applicable share back flag-tagged ahr polyclonal ahr antibodies pennsylvania state university yale university performed cellular biology list open pray-grantb center vanden heuvelb center cos-1 cell cytosol cos-1 cdna library human ahr complexes issue 2 hepatitis ahr-hsp90 complex fourth tpr domains pgem-xap2 constructs hepa 1c1c7 cells information journals a
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articleSection:Transcriptional Regulation
name:Hepatitis B Virus X-Associated Protein 2 Is a Subunit of the Unliganded Aryl Hydrocarbon Receptor Core Complex and Exhibits Transcriptional Enhancer Activity
headline:Hepatitis B Virus X-Associated Protein 2 Is a Subunit of the Unliganded Aryl Hydrocarbon Receptor Core Complex and Exhibits Transcriptional Enhancer Activity
abstract:Prior to ligand activation, the unactivated aryl hydrocarbon receptor (AhR) exists in a heterotetrameric 9S core complex consisting of the AhR ligand-binding subunit, a dimer of hsp90, and an unknown subunit. Here we report the purification of an â¼38-kDa protein (p38) from COS-1 cell cytosol that is a member of this complex by coprecipitation with a FLAG-tagged AhR. Internal amino acid sequence information was obtained, and p38 was identified as the hepatitis B virus X-associated protein 2 (XAP2). The simian ortholog of XAP2 was cloned from a COS-1 cDNA library; it codes for a 330-amino-acid protein containing regions of homology to the immunophilins FKBP12 and FKBP52. A tetratricopeptide repeat (TPR) domain in the carboxy-terminal region of XAP2 was similar to the third and fourth TPR domains of human FKBP52 and the Saccharomyces cerevisiae transcriptional modulator SSN6, respectively. Polyclonal antibodies raised against XAP2 recognized p38 in the unliganded AhR complex in COS-1 and Hepa 1c1c7 cells. It was ubiquitously expressed in murine tissues at the protein and mRNA levels. It was not required for the assembly of an AhR-hsp90 complex in vitro. Additionally, XAP2 did not directly associate with hsp90 upon in vitro translation, but was present in a 9S form when cotranslated in vitro with murine AhR. XAP2 enhanced the ability of endogenous murine and human AhR complexes to activate a dioxin-responsive element–luciferase reporter twofold, following transient expression of XAP2 in Hepa 1c1c7 and HeLa cells.
description:Prior to ligand activation, the unactivated aryl hydrocarbon receptor (AhR) exists in a heterotetrameric 9S core complex consisting of the AhR ligand-binding subunit, a dimer of hsp90, and an unknown subunit. Here we report the purification of an â¼38-kDa protein (p38) from COS-1 cell cytosol that is a member of this complex by coprecipitation with a FLAG-tagged AhR. Internal amino acid sequence information was obtained, and p38 was identified as the hepatitis B virus X-associated protein 2 (XAP2). The simian ortholog of XAP2 was cloned from a COS-1 cDNA library; it codes for a 330-amino-acid protein containing regions of homology to the immunophilins FKBP12 and FKBP52. A tetratricopeptide repeat (TPR) domain in the carboxy-terminal region of XAP2 was similar to the third and fourth TPR domains of human FKBP52 and the Saccharomyces cerevisiae transcriptional modulator SSN6, respectively. Polyclonal antibodies raised against XAP2 recognized p38 in the unliganded AhR complex in COS-1 and Hepa 1c1c7 cells. It was ubiquitously expressed in murine tissues at the protein and mRNA levels. It was not required for the assembly of an AhR-hsp90 complex in vitro. Additionally, XAP2 did not directly associate with hsp90 upon in vitro translation, but was present in a 9S form when cotranslated in vitro with murine AhR. XAP2 enhanced the ability of endogenous murine and human AhR complexes to activate a dioxin-responsive element–luciferase reporter twofold, following transient expression of XAP2 in Hepa 1c1c7 and HeLa cells.
author:
type:Person
name:Brian K. Meyer
type:Person
name:Marilyn G. Pray-Grant
type:Person
name:John P. Vanden Heuvel
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