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    In vitro nuclear interactome of the HIV-1 Tat protein.

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    Authors
    Gautier, Virginie W
    Gu, Lili
    O'Donoghue, Niaobh
    Pennington, Stephen
    Sheehy, Noreen
    Hall, William W
    Affiliation
    UCD-Centre for Research in Infectious Diseases, School of Medicine and Medical Science, University College Dublin (UCD), Belfield, Dublin 4, Ireland. virginie.gautier@ucd.ie
    Issue Date
    2009
    MeSH
    Amino Acid Motifs
    Chromatography, Affinity
    Gene Expression Regulation, Viral
    Gene Regulatory Networks
    HIV Infections
    HIV-1
    Host-Pathogen Interactions
    Humans
    Jurkat Cells
    Mass Spectrometry
    Nuclear Proteins
    RNA Processing, Post-Transcriptional
    RNA, Viral
    tat Gene Products, Human Immunodeficiency Virus
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    Citation
    In vitro nuclear interactome of the HIV-1 Tat protein. 2009, 6:47 Retrovirology
    Journal
    Retrovirology
    URI
    http://hdl.handle.net/10147/94688
    DOI
    10.1186/1742-4690-6-47
    PubMed ID
    19454010
    Abstract
    BACKGROUND: One facet of the complexity underlying the biology of HIV-1 resides not only in its limited number of viral proteins, but in the extensive repertoire of cellular proteins they interact with and their higher-order assembly. HIV-1 encodes the regulatory protein Tat (86-101aa), which is essential for HIV-1 replication and primarily orchestrates HIV-1 provirus transcriptional regulation. Previous studies have demonstrated that Tat function is highly dependent on specific interactions with a range of cellular proteins. However they can only partially account for the intricate molecular mechanisms underlying the dynamics of proviral gene expression. To obtain a comprehensive nuclear interaction map of Tat in T-cells, we have designed a proteomic strategy based on affinity chromatography coupled with mass spectrometry. RESULTS: Our approach resulted in the identification of a total of 183 candidates as Tat nuclear partners, 90% of which have not been previously characterised. Subsequently we applied in silico analysis, to validate and characterise our dataset which revealed that the Tat nuclear interactome exhibits unique signature(s). First, motif composition analysis highlighted that our dataset is enriched for domains mediating protein, RNA and DNA interactions, and helicase and ATPase activities. Secondly, functional classification and network reconstruction clearly depicted Tat as a polyvalent protein adaptor and positioned Tat at the nexus of a densely interconnected interaction network involved in a range of biological processes which included gene expression regulation, RNA biogenesis, chromatin structure, chromosome organisation, DNA replication and nuclear architecture. CONCLUSION: We have completed the in vitro Tat nuclear interactome and have highlighted its modular network properties and particularly those involved in the coordination of gene expression by Tat. Ultimately, the highly specialised set of molecular interactions identified will provide a framework to further advance our understanding of the mechanisms of HIV-1 proviral gene silencing and activation.
    Language
    en
    ISSN
    1742-4690
    ae974a485f413a2113503eed53cd6c53
    10.1186/1742-4690-6-47
    Scopus Count
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