Second-site long terminal repeat (LTR) revertants of replication-defective human immunodeficiency virus: effects of revertant TATA box motifs on virus infectivity, LTR-directed expression, in vitro RNA synthesis, and binding of basal transcription factors TFIID and TFIIA.

1994 ◽  
Vol 68 (5) ◽  
pp. 3298-3307 ◽  
Author(s):  
F Kashanchi ◽  
R Shibata ◽  
E K Ross ◽  
J N Brady ◽  
M A Martin
Keyword(s):  
Human Immunodeficiency Virus ◽  
Transcription Factors ◽  
Long Terminal Repeat ◽  
Rna Synthesis ◽  
Tata Box ◽  
Virus Infectivity ◽  
Basal Transcription ◽  
Immunodeficiency Virus ◽  
Basal Transcription Factors

Transcriptional activation from the long-terminal repeat of human immunodeficiency virus in Vitro

Virology ◽  
1990 ◽  
Vol 177 (2) ◽  
pp. 606-614 ◽  
Author(s):  
Takashi Okamoto ◽  
Thomas Benter ◽  
Steven F. Josephs ◽  
M. Reza Sadaie ◽  
Flossie Wong-Staal
Keyword(s):  
Human Immunodeficiency Virus ◽  
Long Terminal Repeat ◽  
Transcriptional Activation ◽  
Terminal Repeat ◽  
Immunodeficiency Virus

In vitro toxicity and metabolism of 2′,3′-dideoxycytidine, an inhibitor of human immunodeficiency virus infectivity

1991 ◽  
Vol 79 (1) ◽  
pp. 53-64 ◽  
Author(s):  
Giorgio Brandi ◽  
Luigia Rossi ◽  
Giuditta F. Schiavano ◽  
Leonardo Salvaggio ◽  
Amedeo Albano ◽  
...  
Keyword(s):  
Human Immunodeficiency Virus ◽  
In Vitro Toxicity ◽  
Virus Infectivity ◽  
Immunodeficiency Virus

scholarly journals Targeted Derepression of the Human Immunodeficiency Virus Type 1 Long Terminal Repeat by Pyrrole-Imidazole Polyamides

2002 ◽  
Vol 76 (23) ◽  
pp. 12349-12354 ◽  
Author(s):  
Jason J. Coull ◽  
Guocheng He ◽  
Christian Melander ◽  
Victor C. Rucker ◽  
Peter B. Dervan ◽  
...  
Keyword(s):  
Human Immunodeficiency Virus ◽  
Long Terminal Repeat ◽  
Histone Deacetylase ◽  
Human Immunodeficiency Virus Type ◽  
Virus Type ◽  
Terminal Repeat ◽  
Direct Access ◽  
Immunodeficiency Virus

ABSTRACT The host factor LSF represses the human immunodeficiency virus type 1 long terminal repeat (LTR) by mediating recruitment of histone deacetylase. We show that pyrrole-imidazole polyamides targeted to the LTR can specifically block LSF binding both in vitro and within cells via direct access to chromatin, resulting in increased LTR expression.

scholarly journals Characterization of a family of related cellular transcription factors which can modulate human immunodeficiency virus type 1 transcription in vitro.

1994 ◽  
Vol 14 (3) ◽  
pp. 1776-1785 ◽  
Author(s):  
J B Yoon ◽  
G Li ◽  
R G Roeder
Keyword(s):  
Human Immunodeficiency Virus ◽  
Human Immunodeficiency Virus Type ◽  
Virus Type ◽  
Dominant Negative ◽  
Negative Regulator ◽  
Tata Box ◽  
Immunodeficiency Virus ◽  
Hiv 1

LBP-1 is a cellular protein which binds strongly to sequences around the human immunodeficiency virus type 1 (HIV-1) initiation site and weakly over the TATA box. We have previously shown that LBP-1 represses HIV-1 transcription by inhibiting the binding of TFIID to the TATA box. Four similar but distinct cDNAs encoding LBP-1 (LBP-1a, -b, -c, and -d) have been isolated. These are products of two related genes, and each gene encodes two alternatively spliced products. Comparison of the amino acid sequence of LBP-1 with entries in the available protein data bases revealed the identity of LBP-1c to alpha-CP2, an alpha-globin transcription factor. These proteins are also homologous to Drosophila melanogaster Elf-1/NTF-1, an essential transcriptional activator that functions during Drosophila embryogenesis. Three of the recombinant LBP-1 isoforms show DNA binding specificity identical to that of native LBP-1 and bind DNA as a multimer. In addition, antisera raised against recombinant LBP-1 recognize native LBP-1 from HeLa nuclear extract. Functional analyses in a cell-free transcription system demonstrate that recombinant LBP-1 specifically represses transcription from a wild-type HIV-1 template but not from an LBP-1 mutant template. Moreover, LBP-1 can function as an activator both in vivo and in vitro, depending on the promoter context. Interestingly, one isoform of LBP-1 which is missing the region of the Elf-1/NTF-1 homology is unable to bind DNA itself and, presumably through heteromer formation, inhibits binding of the other forms of LBP-1, suggesting that it may function as a dominant negative regulator.

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