scholarly journals Transcriptional activation of the human T-lymphotropic virus type I long terminal repeat by functional interaction of Tax1 and Ets1.

1993 ◽  
Vol 67 (12) ◽  
pp. 7307-7316 ◽  
Author(s):  
S D Gitlin ◽  
J Dittmer ◽  
R C Shin ◽  
J N Brady
Keyword(s):  
Long Terminal Repeat ◽  
Virus Type ◽  
Transcriptional Activation ◽  
Terminal Repeat ◽  
Type I ◽  
Functional Interaction ◽  
T Lymphotropic Virus

scholarly journals Repression of Human T-lymphotropic virus type 1 Long Terminal Repeat sense transcription by Sp1 recruitment to novel Sp1 binding sites

2017 ◽  
Vol 7 (1) ◽  
Author(s):  
Sylvain Fauquenoy ◽  
Gwenaëlle Robette ◽  
Anna Kula ◽  
Caroline Vanhulle ◽  
Sophie Bouchat ◽  
...  
Keyword(s):  
Long Terminal Repeat ◽  
Virus Type ◽  
Binding Sites ◽  
Terminal Repeat ◽  
T Lymphotropic Virus

A 36-kilodalton cellular transcription factor mediates an indirect interaction of human T-cell leukemia/lymphoma virus type I TAX1 with a responsive element in the viral long terminal repeat

1990 ◽  
Vol 10 (8) ◽  
pp. 4192-4201
Author(s):  
S J Marriott ◽  
P F Lindholm ◽  
K M Brown ◽  
S D Gitlin ◽  
J F Duvall ◽  
...  
Keyword(s):  
T Cell ◽  
Long Terminal Repeat ◽  
Virus Type ◽  
Terminal Repeat ◽  
Type I ◽  
Indirect Interaction ◽  
T Cell Leukemia ◽  
Cell Leukemia ◽  
Human T Cell ◽  
Responsive Element

The human T-cell leukemia/lymphoma virus type I (HTLV-I) trans activator, TAX1, interacts indirectly with a TAX1-responsive element, TRE-2, located at positions -117 to -163 in the viral long terminal repeat. This report describes the characterization of a 36-kilodalton (kDa) protein identified in HeLa nuclear extract which mediates the interaction of TAX1 with TRE-2. Purification of the protein was achieved by zinc chelate chromatography and preparative sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The renatured 36-kDa protein bound specifically to a TRE-2 oligonucleotide but not to nonfunctional base substitution mutant probes in a gel retardation assay. Renatured proteins of differing molecular weights were unable to form this complex. In addition, the 36-kDa protein specifically activated transcription from the HTLV-I promoter in vitro. Purified TAX1 protein formed a complex with the TRE-2 oligonucleotide in the presence of the 36-kDa protein, suggesting that indirect interaction of TAX1 with the viral long terminal repeat may be one of the mechanisms by which HTLV-I transcription is regulated.

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