HEED, the Product of the Human Homolog of the Murineeed Gene, Binds to the Matrix Protein of HIV-1

Peytavi, Régis; Hong, Saw See; d’Angeac, Arnaud Dupuy; Selig, Luc; Bénichou, Serge; Bénarous, Richard; Boulanger, Pierre

doi:10.1074/jbc.274.3.1635

Cited by 43 publications

(52 citation statements)

References 72 publications

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“…Another possibility is that the cellular proteins recruited by specific histone posttranslational modifications tether integration complexes near sites of modification. HIV-1 integrase has been reported to bind to several chromatin-associated proteins (Kalpana et al 1994;Peytavi et al 1999), providing candidate ligands. Alternatively, epigenetic modifications may be only markers of favored integration sites and not directly involved in the targeting mechanism.…”

Section: Discussionmentioning

confidence: 99%

HIV integration site selection: Analysis by massively parallel pyrosequencing reveals association with epigenetic modifications

Wang¹,

Ciuffi²,

Leipzig³

et al. 2007

Genome Res.

413

491

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Integration of retroviral DNA into host cell DNA is a defining feature of retroviral replication. HIV integration is known to be favored in active transcription units, which promotes efficient transcription of the viral genes, but the molecular mechanisms responsible for targeting are not fully clarified. Here we used pyrosequencing to map 40,569 unique sites of HIV integration. Computational prediction of nucleosome positions in target DNA indicated that integration sites are periodically distributed on the nucleosome surface, consistent with favored integration into outward-facing DNA major grooves in chromatin. Analysis of integration site positions in the densely annotated ENCODE regions revealed a wealth of new associations between integration frequency and genomic features. Integration was particularly favored near transcription-associated histone modifications, including H3 acetylation, H4 acetylation, and H3 K4 methylation, but was disfavored in regions rich in transcription-inhibiting modifications, which include H3 K27 trimethylation and DNA CpG methylation. Statistical modeling indicated that effects of histone modification on HIV integration were partially independent of other genomic features influencing integration. The pyrosequencing and bioinformatic methods described here should be useful for investigating many aspects of retroviral DNA integration.

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Section: Discussionmentioning

confidence: 99%

HIV integration site selection: Analysis by massively parallel pyrosequencing reveals association with epigenetic modifications

Wang¹,

Ciuffi²,

Leipzig³

et al. 2007

Genome Res.

413

491

View full text Add to dashboard Cite

show abstract

“…Previous reports, mostly based on northern analysis of adult tissues and cell lines, indicated widespread mRNA expression of eed and Bmi1 (Schumacher et al, 1996;Alkema et al, 1997a;Denisenko and Bomsztyk, 1997;Gunster et al, 1997;Denisenko et al, 1998;Rietzler et al, 1998;Schumacher et al, 1998;Sewalt et al, 1998;Peytavi et al, 1999). mRNA in situ hybridization studies detected coexpression of eed and Bmi1 in somites and neuroectoderm in E8.5 wild-type embryos (Fig.…”

Section: Coexpression Of Eed and Bmi1 In Somites And Neuroectodermmentioning

confidence: 99%

Juxtaposed Polycomb complexes co-regulate vertebral identity

Kim

Magnuson

et al. 2006

Development

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Best known as epigenetic repressors of developmental Hox gene transcription, Polycomb complexes alter chromatin structure by means of post-translational modification of histone tails. Depending on the cellular context, Polycomb complexes of diverse composition and function exhibit cooperative interaction or hierarchical interdependency at target loci. The present study interrogated the genetic, biochemical and molecular interaction of BMI1 and EED, pivotal constituents of heterologous Polycomb complexes, in the regulation of vertebral identity during mouse development. Despite a significant overlap in dosage-sensitive homeotic phenotypes and co-repression of a similar set of Hox genes, genetic analysis implicated eed and Bmi1 in parallel pathways, which converge at the level of Hox gene regulation. Whereas EED and BMI1 formed separate biochemical entities with EzH2 and Ring1B, respectively, in mid-gestation embryos, YY1 engaged in both Polycomb complexes. Strikingly, methylated lysine 27 of histone H3 (H3-K27), a mediator of Polycomb complex recruitment to target genes, stably associated with the EED complex during the maintenance phase of Hox gene repression. Juxtaposed EED and BMI1 complexes, along with YY1 and methylated H3-K27, were detected in upstream regulatory regions of Hoxc8 and Hoxa5. The combined data suggest a model wherein epigenetic and genetic elements cooperatively recruit and retain juxtaposed Polycomb complexes in mammalian Hox gene clusters toward coregulation of vertebral identity.

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“…The PBL cDNA library was constructed in frame with the cDNA of the Gal4 activating domain in the pGAD1318 vector as described (Peytavi et al, 1999). cDNAs encoding either the full length hDlg protein, or the region containing the three PDZ domains were subcloned from the pCDNA3-hDlg vector (Lue et al, 1994) in the pGAD1318 vector.…”

Section: Methodsmentioning

confidence: 99%

Human Dlg protein binds to the envelope glycoproteins of human T-cell leukemia virus type 1 and regulates envelope mediated cell-cell fusion in T lymphocytes

Blot

Delamarre

Perugi

et al. 2004

Journal of Cell Science

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Human homologue of the Drosophila Dlg tumor suppressor (hDlg) is a widely expressed scaffold protein implicated in the organization of multi-protein complexes at cell adhesion sites such as the neuronal synapse. hDlg contains three PDZ domains that mediate its binding to the consensus motifs present at the C-termini of various cell surface proteins, thus inducing their clustering and/or stabilization at the plasma membrane. Using a yeast two-hybrid screen, we identified hDlg as a cellular binding partner of a viral membrane integral protein, the envelope glycoprotein (Env) of human T-cell leukemia virus type 1 (HTLV-1). HTLV-1 is a human retrovirus that infects CD4+ T lymphocytes and is preferentially transmitted via direct contacts between infected and target cells, through a structure referred to as the virological synapse. Here, we demonstrate that hDlg interacts with a classical PDZ domain-binding motif present at the C-terminus of the cytoplasmic domain of HTLV-1 Env and conserved in the related HTLV-2 virus. We further document that, in HTLV-1 infected primary T cells, hDlg and Env are concentrated in restricted areas of the plasma membrane, enriched in molecules involved in T-cell contacts. The presence of Gag proteins responsible for viral assembly and budding in these areas indicated that they constitute platforms for viral assembly and transmission. Finally, a mutant virus unable to bind hDlg exhibited a decreased ability to trigger Env mediated cell fusion between T lymphocytes. We thus propose that hDlg stabilizes HTLV-1 envelope glycoproteins at the virological synapse formed between infected and target cells, hence assisting the cell-to-cell transmission of the virus.

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HEED, the Product of the Human Homolog of the Murineeed Gene, Binds to the Matrix Protein of HIV-1

Cited by 43 publications

References 72 publications

HIV integration site selection: Analysis by massively parallel pyrosequencing reveals association with epigenetic modifications

HIV integration site selection: Analysis by massively parallel pyrosequencing reveals association with epigenetic modifications

Juxtaposed Polycomb complexes co-regulate vertebral identity

Human Dlg protein binds to the envelope glycoproteins of human T-cell leukemia virus type 1 and regulates envelope mediated cell-cell fusion in T lymphocytes

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