The intracisternal A-particle upstream element interacts with transcription factor YY1 to activate transcription: pleiotropic effects of YY1 on distinct DNA promoter elements

1993 ◽  
Vol 13 (11) ◽  
pp. 6621-6628
Author(s):  
K Satyamoorthy ◽  
K Park ◽  
M L Atchison ◽  
C C Howe
Keyword(s):  
Zinc Finger Protein ◽  
Leukemia Virus ◽  
Cpg Methylation ◽  
Binding Assays ◽  
Long Terminal Repeats ◽  
Enhancer Activity ◽  
Immunoglobulin Kappa ◽  
F9 Embryonal Carcinoma Cells ◽  
Intracisternal A Particle ◽  
Transcription Factor Yy1

Murine intracisternal A-particle long terminal repeats contain an intracisternal A-particle upstream enhancer (IUE) element that binds to a 65-kDa IUE binding protein (IUEB) present in both undifferentiated F9 embryonal carcinoma cells and differentiated parietal endoderm-like PYS-2 cells. This IUE element confers a CpG methylation-sensitive IUEB binding and enhancer activity. Using gel retardation, methylation interference, CpG methylation sensitivity binding, and cotransfection assays, we have now identified the 65-kDa IUEB as YY1 (also called NF-E1, delta, or UCRBP), a zinc finger protein related to the Krüppel family. YY1 binds to a number of similar but distinct DNA motifs, and cotransfection assays indicate that these motifs have different enhancer potentials in PYS-2 cells. The relative strengths of these elements are as follows: IUE > kappa E3' from the human immunoglobulin kappa light-chain 3' enhancer > upstream conserved region from the Moloney murine leukemia virus promoter. Results of DNA binding assays suggest that the differences in enhancer potentials are due to the different binding affinities of YY1 to the various motifs and the binding of two other transcription factors to the IUE sequence.

scholarly journals The intracisternal A-particle upstream element interacts with transcription factor YY1 to activate transcription: pleiotropic effects of YY1 on distinct DNA promoter elements.

1993 ◽  
Vol 13 (11) ◽  
pp. 6621-6628 ◽  
Author(s):  
K Satyamoorthy ◽  
K Park ◽  
M L Atchison ◽  
C C Howe
Keyword(s):  
Zinc Finger Protein ◽  
Leukemia Virus ◽  
Cpg Methylation ◽  
Binding Assays ◽  
Long Terminal Repeats ◽  
Enhancer Activity ◽  
Immunoglobulin Kappa ◽  
F9 Embryonal Carcinoma Cells ◽  
Intracisternal A Particle ◽  
Transcription Factor Yy1

Murine intracisternal A-particle long terminal repeats contain an intracisternal A-particle upstream enhancer (IUE) element that binds to a 65-kDa IUE binding protein (IUEB) present in both undifferentiated F9 embryonal carcinoma cells and differentiated parietal endoderm-like PYS-2 cells. This IUE element confers a CpG methylation-sensitive IUEB binding and enhancer activity. Using gel retardation, methylation interference, CpG methylation sensitivity binding, and cotransfection assays, we have now identified the 65-kDa IUEB as YY1 (also called NF-E1, delta, or UCRBP), a zinc finger protein related to the Krüppel family. YY1 binds to a number of similar but distinct DNA motifs, and cotransfection assays indicate that these motifs have different enhancer potentials in PYS-2 cells. The relative strengths of these elements are as follows: IUE > kappa E3' from the human immunoglobulin kappa light-chain 3' enhancer > upstream conserved region from the Moloney murine leukemia virus promoter. Results of DNA binding assays suggest that the differences in enhancer potentials are due to the different binding affinities of YY1 to the various motifs and the binding of two other transcription factors to the IUE sequence.

Transposition of two different intracisternal A particle elements into an immunoglobulin kappa-chain gene

1984 ◽  
Vol 4 (12) ◽  
pp. 2565-2572
Author(s):  
R G Hawley ◽  
M J Shulman ◽  
N Hozumi
Keyword(s):  
Primer Binding Site ◽  
Chain Gene ◽  
Direct Repeats ◽  
Long Terminal Repeats ◽  
Single Nucleotide ◽  
Immunoglobulin Kappa ◽  
Kappa Chain ◽  
Trna Primer ◽  
Terminal Repeats ◽  
Intracisternal A Particle

Each of two severely defective mouse kappa-chain genes has acquired a different intracisternal A particle (IAP) element within one of its introns. One IAP element generated 6-base-pair direct repeats upon insertion. In contrast, the other IAP element was not flanked by direct repeats and was missing a single nucleotide from its 3' terminus. Sequence analysis of the latter IAP element demonstrated that its long terminal repeats were not identical. Nevertheless, the long terminal repeats were organized like proviral long terminal repeats, and this IAP element did contain two regions that were analogous to retroviral priming sites for RNA-directed DNA synthesis. The region that corresponded to a retroviral tRNA primer binding site was complementary to the 3' ends of all mammalian phenylalanine tRNAs. These findings are discussed in the context of the presumed mode of transposition of IAP elements involving the reverse transcription of IAP RNA.

scholarly journals Transposition of two different intracisternal A particle elements into an immunoglobulin kappa-chain gene.

1984 ◽  
Vol 4 (12) ◽  
pp. 2565-2572 ◽  
Author(s):  
R G Hawley ◽  
M J Shulman ◽  
N Hozumi
Keyword(s):  
Primer Binding Site ◽  
Chain Gene ◽  
Direct Repeats ◽  
Long Terminal Repeats ◽  
Single Nucleotide ◽  
Immunoglobulin Kappa ◽  
Kappa Chain ◽  
Trna Primer ◽  
Terminal Repeats ◽  
Intracisternal A Particle

Each of two severely defective mouse kappa-chain genes has acquired a different intracisternal A particle (IAP) element within one of its introns. One IAP element generated 6-base-pair direct repeats upon insertion. In contrast, the other IAP element was not flanked by direct repeats and was missing a single nucleotide from its 3' terminus. Sequence analysis of the latter IAP element demonstrated that its long terminal repeats were not identical. Nevertheless, the long terminal repeats were organized like proviral long terminal repeats, and this IAP element did contain two regions that were analogous to retroviral priming sites for RNA-directed DNA synthesis. The region that corresponded to a retroviral tRNA primer binding site was complementary to the 3' ends of all mammalian phenylalanine tRNAs. These findings are discussed in the context of the presumed mode of transposition of IAP elements involving the reverse transcription of IAP RNA.

Binding of a cellular protein to the gibbon ape leukemia virus enhancer

1987 ◽  
Vol 7 (8) ◽  
pp. 2735-2744
Author(s):  
J P Quinn ◽  
N Holbrook ◽  
D Levens
Keyword(s):  
Long Terminal Repeat ◽  
Specific Binding ◽  
Leukemia Virus ◽  
Cellular Protein ◽  
Terminal Repeat ◽  
Enhancer Activity ◽  
Repeated Element ◽  
Gibbon Ape Leukemia Virus

The gibbon ape leukemia virus (GALV) contains enhancer activity within its long terminal repeat. In the GALV Seato strain this activity resides in a 48-base-pair (bp) repeated element. We demonstrate the existence of a cellular protein which binds in this region of the Seato strain. A sensitive method for enriching protein-DNA complexes from crude extracts coupled with exonuclease and DNase footprint analysis revealed the specific binding of this protein to a 21-bp region within each repeated element. A 22-bp oligonucleotide fragment defined solely by the 21-bp footprint binds a protein in vitro and displays enhancer activity in vivo, suggesting that this protein is a major determinant of GALV enhancer activity. The protein is present in three cell lines which are positive for enhancer activity and is not detected in Jurkat cells, which are negative for enhancer activity. Only GALV long-terminal-repeat variants which support high levels of enhancer activity in vivo compete with this protein for specific binding in vitro, suggesting a potential role for the protein in determining enhancer activity. This protein binding is not inhibited by competition with heterologous retroviral enhancers, demonstrating that it is not a ubiquitous retroviral enhancer binding protein.

scholarly journals Identification of Homeodomain Proteins, PBX1 and PREP1, Involved in the Transcription of Murine Leukemia Virus

2003 ◽  
Vol 23 (3) ◽  
pp. 831-841 ◽  
Author(s):  
Sheng-Hao Chao ◽  
John R. Walker ◽  
Sumit K. Chanda ◽  
Nathanael S. Gray ◽  
Jeremy S. Caldwell
Keyword(s):  
Murine Leukemia Virus ◽  
Kinase Inhibitors ◽  
Leukemia Virus ◽  
Moloney Murine Leukemia Virus ◽  
Viral Transcription ◽  
Long Terminal Repeats ◽  
Homeodomain Proteins ◽  
Cellular Genes ◽  
Simplex Virus ◽  
Murine Leukemia

ABSTRACT Cyclin-dependent kinase inhibitors (CDKIs) have been shown to block human immunodeficiency virus and herpes simplex virus. It is hypothesized that CDKIs block viral replication by inhibiting transcription of specific cellular genes. Here we find that three CDKIs, flavopiridol, purvalanol A, and methoxy-roscovitine, block Moloney murine leukemia virus (MLV) transcription events. Using gene expression microarray technology to examine the inhibitory effects of CDKIs, we observed a cellular gene, the pre-B-cell leukemia transcription factor 1 (Pbx1) gene, down-regulated by CDKI treatment. The PBX consensus element (PCE), TGATTGAC, is conserved in the long terminal repeats of several murine retroviruses, including Moloney MLV. Mutations in the PCE completely inhibited viral transcription whereas overexpression of PBX1 and a PBX1-associated protein, PREP1, enhanced viral transcription. The interaction between the PCE and PBX1-PREP1 proteins was confirmed by gel shift experiments. Blocking PBX1 protein synthesis resulted in a significant decrease in viral transcription. Collectively, our results represent the first work demonstrating that the homeodomain proteins PBX1 and PREP1 are cellular factors involved in Moloney MLV transcription regulation.

scholarly journals Group I p21-activated kinases facilitate Tax-mediated transcriptional activation of the human T-cell leukemia virus type 1 long terminal repeats

Retrovirology ◽  
2013 ◽  
Vol 10 (1) ◽  
pp. 47 ◽  
Author(s):  
Ching-Ping Chan ◽  
Yeung-Tung Siu ◽  
Kin-Hang Kok ◽  
Yick-Pang Ching ◽  
Hei-Man Vincent Tang ◽  
...  
Keyword(s):  
T Cell ◽  
Transcriptional Activation ◽  
Leukemia Virus ◽  
Cell Leukemia ◽  
Long Terminal Repeats ◽  
Cell Leukemia Virus Type ◽  
Human T Cell ◽  
Group I ◽  
T Cell Leukemia Virus

Selective expression of intracisternal A-particle genes in established mouse plasmacytomas

1993 ◽  
Vol 13 (12) ◽  
pp. 7439-7446
Author(s):  
K K Lueders ◽  
J W Fewell ◽  
V E Morozov ◽  
E L Kuff
Keyword(s):  
B Cells ◽  
Regulatory Sequence ◽  
Cdna Clones ◽  
Sequence Variants ◽  
Long Terminal Repeats ◽  
Specific Sequence ◽  
Rna Transcripts ◽  
Sequence Selection ◽  
Intracisternal A Particle ◽  
Rna Blots

Mouse plasmacytomas generally express higher levels of RNA transcripts from endogenous intracisternal A-particle (IAP) proviral elements than do lipopolysaccharide-stimulated normal lymphocytes. Lymphocytes express a limited and highly characteristic set of IAP elements (lymphocyte-specific [LS] elements). In this study, we examined whether LS elements are expressed at higher levels after transformation of the cells and/or whether new IAP elements are activated. The IAP elements expressed in plasmacytoma MPC11 were characterized by sequence analysis of 22 cDNA clones. The long terminal repeats (LTRs) of the tumor cDNAs proved to be highly related in sequence. None of the clones was of the LS cDNA type. The MPC11 LTRs were five- to sixfold more active than an LS cDNA LTR when tested for promoter activity by transfection into plasmacytoma cells. The LTRs of the tumor-derived cDNAs contained a canonical ATF core sequence (ATF-PC), while the LS cDNAs contained an altered sequence (ATF-LS). An ATF-PC oligonucleotide probe detected multiple IAP transcripts on Northern (RNA) blots of RNA from several plasmacytoma but gave no reaction with RNA from stimulated B lymphocytes. In contrast, an ATF-LS probe detected higher levels of RNA in lymphocyte than in tumor RNAs. Thus, expression of IAP elements in transformed B cells is selective for a different set of regulatory sequence variants than those expressed in normal B cells. Other oligonucleotide probes representing LS- and PC-specific sequence variants detected multiple common hypomethylated IAP proviral loci in three independently derived plasmacytomas. Overall, the results show that established plasmacytomas exhibit a characteristic pattern of IAP proviral hypomethylation and regulatory sequence selection.

Functional analysis of the long terminal repeats of intracisternal A-particle genes: sequences within the U3 region determine both the efficiency and direction of promoter activity

1988 ◽  
Vol 8 (3) ◽  
pp. 1093-1102
Author(s):  
R J Christy ◽  
R C Huang
Keyword(s):  
Reporter Gene ◽  
Promoter Activity ◽  
Transcriptional Activity ◽  
Antisense Transcription ◽  
Regulatory Elements ◽  
Deletion Mapping ◽  
Long Terminal Repeats ◽  
Terminal Repeats ◽  
Nuclease Mapping ◽  
Intracisternal A Particle

The transcriptional activity of five intracisternal A-particle (IAP) long terminal repeats (LTRs) in mouse embryonal carcinoma PCC3-A/1 cells and in Ltk- cells was determined. We tested the promoter activity of the LTRs by coupling them to the reporter gene chloramphenicol acetyltransferase (CAT) or guanosine-xanthine phosphoribosyltransferase (gpt). Each LTR was tested for promoter function in both the sense (5' to 3') and antisense (3' to 5') orientation preceding the reporter gene. The transcriptional activity of individual IAP gene LTRs varied considerably, and the LTR from IAP81 possessed promoter activity in both directions. The bidirectional activity of the IAP81 LTR confirmed by monitoring Ecogpt expression in stably transfected Ltk- cells, with the initiation sites for sense and antisense transcription being localized to within the IAP81 LTR by S1 nuclease mapping. Deletions of LTR81 show that for normal 5'-to-3' gene transcription (sense direction), the 3'U3/R region determines the basal level of transcription, whereas sequences within the 5'U3 region enhance transcription four- to fivefold. Deletion mapping for antisense transcription indicates that a 64-base-pair region (nucleotides 47 to 110) within the U3 region is essential for activity. These data indicate that the U3 region contains all the regulatory elements for bidirectional transcription in IAP LTRs.

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