Nucleic Acids Research, 2000, Vol. 28, No. 3 663-668
© 2000 Oxford University Press
SURVEY AND SUMMARY A compilation of cellular transcription factor interactions with the HIV-1 LTR promoter
AIDS Molecular Biology Unit, National Centre for HIV Virology Research, The Macfarlane Burnet Centre for Medical Research, PO Box 254, Fairfield, Victoria 3078, Australia
Received October 5, 1999; Accepted November 4, 1999.
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ABSTRACT |
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 TOP ABSTRACT INTRODUCTIONDESCRIPTION OF THE COMPILATIONREFERENCES |
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The human immunodeficiency virus type 1 (HIV-1) long terminal repeat (LTR) represents a model promoter system and the identification and characterisation of cellular proteins that interact with this region has provided a basic understanding about both general eukaryotic and HIV-1 proviral transcriptional regulation. To date a large number of sequence-specific DNA–protein interactions have been described for the HIV-1 LTR. The aim of this report is to provide a comprehensive, updated listing of these HIV-1 LTR interactions. It is intended as a reference point to facilitate on-going studies characterising the identity of cellular proteins interacting with the HIV-1 LTR and the functional role(s) of specific regions of the LTR for HIV-1 replication.
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INTRODUCTION |
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TOPABSTRACTINTRODUCTIONDESCRIPTION OF THE COMPILATIONREFERENCES |
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The regulation of human immunodeficiency virus type 1 (HIV-1) proviral gene expression is tightly regulated by the binding of cellular host proteins to a variety of cis-acting DNA sequences located within the long terminal repeat (LTR) region of the viral genome (1). The HIV-1 LTR is divided into three regions: U3, R and U5 (Fig. 1). These contain four functional regions related to the regulation of HIV-1 transcription: the transactivation response (TAR) element found within R (nt +1 to +60), the basal or core promoter (nt –78 to –1), a core enhancer (nt –105 to –79) and a modulatory region (nt –454 to –104) (1). The last three are found within U3. The modulatory region has also been proposed to contain a negative regulatory element (NRE) between nt –340 and –184 because deletions within this region increased HIV-1 LTR-directed transcription and viral replication (2,3).
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Early reports showed the three Sp1 core promoter binding sites and two NF-
B core enhancer motifs to be key elements involved in the regulation of HIV-1 transcription (1). Several cellular proteins including c-Myb, NF-AT, USF and COUP have also been proposed to interact with the modulatory region and contribute to HIV-1 LTR promoter activity (1,4–7). Subsequent studies have revealed a wealth of additional U3 and TAR DNA–protein interactions that significantly influence levels of HIV-1 LTR transcription. More recently, important motifs within the U5 region and gag leader sequence (GLS) have been described (8–11). Furthermore, we have identified a fourth Sp1 binding site at the 5'-end of the U3 region and, in addition to the U3 USF and NF-B sites, found it to be essential for negative sense transcription from the HIV-1 LTR (12,13). Together these various binding sites and their relative orientations mediate combinatorial DNA–protein and protein–protein interactions that form a complex regulatory network through which HIV-1 regulates its levels of positive and negative sense gene expression in a diverse range of target host cells under a variety of extracellular stimuli. |
DESCRIPTION OF THE COMPILATION |
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TOPABSTRACTINTRODUCTIONDESCRIPTION OF THE COMPILATIONREFERENCES |
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The present report provides an updated listing covering previously published HIV-1 LTR DNA–protein interactions (Tables 1–5). Interactions are tabulated according to the functional regions of the LTR (R/U5 junction, U5, GLS, TAR, basal/core promoter, core enhancer and modulatory region). The identity and site of interaction are listed in the first and second columns, respectively. Within each table interactions are listed in an order that is relative to the transcription start site +1. While most interactions are highly conserved across strains of HIV-1, not all sites are found in all strains and the exact position of an interacting site may differ slightly. Therefore, sites are recorded according to the numbering of the HIV-1 strain used in the original description. The source cell type and stimulatory conditions under which the interaction was observed are listed in the third column. In some instances interactions have been defined using only proteins in either a recombinant or purified form. For each interaction, the effect on levels of HIV-1 LTR transcription is provided in the fourth column. For more specific details of transcription factor interactions with the HIV-1 LTR and their proposed effect(s) on levels of transcription readers are referred to publications cited in the fifth column.
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ACKNOWLEDGEMENTS |
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We are grateful to members of the AIDS Molecular Biology Unit, in particular Paul F. Lambert and Mandy Ludford-Menting, for helpful discussions and assistance. We thank Prof. John Mills for critical review of the manuscript. L.A.P. was in receipt of a Commonwealth AIDS Research Grant PhD Scholarship. Work in the AIDS Molecular Biology Unit is supported by an Australian Commonwealth AIDS Research Grant as a Laboratory of the National Centre in HIV Virology Research and the Research Fund of the Macfarlane Burnet Centre for Medical Research.
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FOOTNOTES |
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* To whom correspondence should be addressed. Tel: +61 3 9282 2234; Fax: +61 3 9482 6152; Email: deacon@burnet.edu.au Present addresses: Lloyd A. Pereira, Laboratory for Physiological Chemistry, Utrecht University, Universiteitsweg 100, 3584G CG Utrecht, The Netherlands Anna Peeters, Department of Epidemiology and Preventive Medicine, Monash Medical School, Alfred Hospital, Prahran, Victoria 3181, Australia
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D. G. Brooks, P. A. Arlen, L. Gao, C. M. R. Kitchen, and J. A. Zack Identification of T cell-signaling pathways that stimulate latent HIV in primary cells PNAS, October 28, 2003; 100(22): 12955 - 12960. [Abstract] [Full Text] [PDF]
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O. Rohr, D. Lecestre, S. Chasserot-Golaz, C. Marban, D. Avram, D. Aunis, M. Leid, and E. Schaeffer Recruitment of Tat to Heterochromatin Protein HP1 via Interaction with CTIP2 Inhibits Human Immunodeficiency Virus Type 1 Replication in Microglial Cells J. Virol., May 1, 2003; 77(9): 5415 - 5427. [Abstract] [Full Text] [PDF]
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N. E. Faulkner, B. R. Lane, P. J. Bock, and D. M. Markovitz Protein Phosphatase 2A Enhances Activation of Human Immunodeficiency Virus Type 1 by Phorbol Myristate Acetate J. Virol., February 1, 2003; 77(3): 2276 - 2281. [Abstract] [Full Text] [PDF]
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B. M. Badran, S. M. Wolinsky, A. Burny, and K. E. Willard-Gallo Identification of Three NFAT Binding Motifs in the 5'-Upstream Region of the Human CD3gamma Gene That Differentially Bind NFATc1, NFATc2, and NF-kappa B p50 J. Biol. Chem., November 27, 2002; 277(49): 47136 - 47148. [Abstract] [Full Text] [PDF]
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V. Quivy, E. Adam, Y. Collette, D. Demonte, A. Chariot, C. Vanhulle, B. Berkhout, R. Castellano, Y. de Launoit, A. Burny, et al. Synergistic Activation of Human Immunodeficiency Virus Type 1 Promoter Activity by NF-{kappa}B and Inhibitors of Deacetylases: Potential Perspectives for the Development of Therapeutic Strategies J. Virol., October 2, 2002; 76(21): 11091 - 11103. [Abstract] [Full Text] [PDF]
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B. Wortman, N. Darbinian, B. E. Sawaya, K. Khalili, and S. Amini Evidence for Regulation of Long Terminal Repeat Transcription by Wnt Transcription Factor TCF-4 in Human Astrocytic Cells J. Virol., October 2, 2002; 76(21): 11159 - 11165. [Abstract] [Full Text] [PDF]
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Y. Liu, J. Li, B. O. Kim, B. S. Pace, and J. J. He HIV-1 Tat Protein-mediated Transactivation of the HIV-1 Long Terminal Repeat Promoter Is Potentiated by a Novel Nuclear Tat-interacting Protein of 110 kDa, Tip110 J. Biol. Chem., June 21, 2002; 277(26): 23854 - 23863. [Abstract] [Full Text] [PDF]
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