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Volumn 273, Issue 5277, 1996, Pages 951-953

Exclusion of Int-6 from PML nuclear bodies by binding to the HTLV-I Tax oncoprotein

Author keywords

[No Author keywords available]

Indexed keywords

TAX PROTEIN;

EID: 0029789753     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.273.5277.951     Document Type: Article
Times cited : (130)

References (40)
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    • We used the MATCHMAKER two-hybrid system (Clontech, Palo Alto, CA). The Tax coding sequence was fused to the GAL4 DNA binding domain into the pGB-T9 yeast expression vector, giving pGB-Tax. The human cDNA library we used has been described (5). Briefly, cDNAs from EBV-transformed human peripheral lymphocytes were fused to the GAL4 transcriptional activation domain into the λACT phage vector. pGB-Tax was introduced into the HF7c yeast strain, and the resulting cells were transformed by the fusion cDNA library. The HF7c strain possesses the His synthetase gene (HIS3) and the lacZ gene under the control of GAL4 binding sites. From an initial screen of 250,000 transformants, 700 were found to grow on a minimal medium lacking His. Of these, 94 were also positive when assayed for β-galactosidase expression. Plasmid DNAs from the double positive clones were extracted and sequenced.
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    • 6) were transfected by the calcium phosphate precipitation method with 1 μg of the pG4G3CAT reporter construct (8), 10 ng of pG4M or pSG4-Tax (8), and 100 ng of pSG-FNV or pSG-FNV-70. pSG-FNV is a pSG5 derivative encoding the FLAG epitope fused to the SV40 nuclear localization signal and to the VP16 activation domain (amino acids 403 to 479). The clone 70 Int-6 cDNA was inserted into this parental plasmid to give pSG-FNV-70. Duplicate transfections were done for each combination of plasmids Forty hours after transfection, concentrations of the CAT protein were measured by enzyme-linked immunosorbent assay (Boehringer Mannheim).
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    • 6) were transfected with 1 μg of pSGF-Int-6 or 1 μg of pSG-Tax, or both. Cells were lysed in radioimmunoprecipitation assay buffer. The immunoprecipitates were separated on a 10% polyacrylamide-SDS gel and blotted onto nitrocellulose. The enhanced chemiluminescent detection system (ECL, Amersham) was used to visualize bound antibodies.
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    • We generated a polyclonal rabbit antiserum to a peptide corresponding to the COOH-terminal 20 amino acids of Int-6 coupled to ovalbumin. To purify this serum, we produced a FLAG-Int-6 fusion protein in bacteria and coupled it to a FLAG M2 antibody affinity gel (Kodak). Covalent linkage between the protein and the M2 antibody was performed by treatment with glutaraldehyde. The antiserum to Int-6 was incubated with this matrix, and specific antibodies were eluted with 100 mM glycine (pH 2.5).
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    • We thank S. Elledge for providing the cDNA library; B. Cullen for the antiserum to Tax; A. Dejean for the PML rabbit polyclonal serum; R. van Driel for the PML monoclonal antibody; P. Chambon for the PML expression vector; C. Souchier for help with confocal microscopy; F. Chatelet for assistance in preparing the figures; and J. Maryanski for critical reading of the manuscript. This work was supported by the Agence Nationale de Recherches sur le Sida and the Association pour la Recherche contre le Cancer (F.B.).


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