NDLI: Hepatitis B Virus X-Associated Protein 2 Is a Subunit of the Unliganded Aryl Hydrocarbon Receptor Core Complex and Exhibits Transcriptional Enhancer Activity

Content Provider	PubMed Central
Author	Meyer, Brian K. Pray-grant, Marilyn G. Heuvel, John P. Vanden Perdew, Gary H.
Copyright Year	1998
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 ∼38-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.
Starting Page	978
File Format	PDF
ISSN	10985549
e-ISSN	10985549
Journal	Molecular and Cellular Biology
Issue Number	2
Volume Number	18
Language	English
Publisher	American Society for Microbiology
Publisher Date	1998-02-01
Access Restriction	Open
Rights Holder	American Society for Microbiology
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Cell Biology Molecular Biology

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The Aryl Hydrocarbon (Ah) Receptor Transcriptional Regulator Hepatitis B Virus X-associated Protein 2 Antagonizes p23 Binding to Ah Receptor-Hsp90 Complexes and Is Dispensable for Receptor Function

Subcellular Localization of the Aryl Hydrocarbon Receptor Is Modulated by the Immunophilin Homolog Hepatitis B Virus X-associated Protein 2

The hsp90 Co-chaperone XAP2 Alters Importin β Recognition of the Bipartite Nuclear Localization Signal of the Ah Receptor and Represses Transcriptional Activity

Recruitment of the NCoA/SRC-1/p160 Family of Transcriptional Coactivators by the Aryl Hydrocarbon Receptor/Aryl Hydrocarbon Receptor Nuclear Translocator Complex

Hepatitis B Virus X Protein Is a Transcriptional Modulator That Communicates with Transcription Factor IIB and the RNA Polymerase II Subunit 5

Identification of protein-binding sites in the hepatitis B virus enhancer and core promoter domains.

Subunit composition of the heteromeric cytosolic aryl hydrocarbon receptor complex.

Interaction of Hepatitis B Viral X Protein and CCAAT/ Enhancer-binding Protein α Synergistically Activates the Hepatitis B Viral Enhancer II/Pregenomic Promoter

The Q-rich Subdomain of the Human AhReceptor Transactivation Domain Is Required for Dioxin-mediated Transcriptional Activity

Hepatitis B Virus X-Associated Protein 2 Is a Subunit of the Unliganded Aryl Hydrocarbon Receptor Core Complex and Exhibits Transcriptional Enhancer Activity

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