Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0021051 (immunodeficiency)
 71,517 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We have shown by site-directed mutagenesis that the sequence between positions -69 and -40 of the mouse alpha A-crystallin gene is crucial for tissue-specific gene expression in a transfected mouse lens epithelial cell line transformed with the early region of simian virus 40. Gel retardation experiments with synthetic oligodeoxynucleotides revealed a mouse lens nuclear protein which bound specifically to the palindromic sequence 5'-GGGAAATCCC-3' at positions -66 to -57 in the alpha A-crystallin promoter. By screening a bacteriophage lambda gt11 expression library of the transformed lens cells, we isolated a 2.5-kilobase-pair cDNA encoding a fusion protein which bound to this sequence and to the regulatory element of the major histocompatibility complex (MHC) class I gene. This cDNA hybridized to a 10-kilobase-pair polyadenylated RNA present in many different tissues, including lens. It encoded a protein, tentatively called alpha A-CRYBP1, containing at least two zinc fingers. alpha A-CRYBP1 is either homologous or very similar to the human nuclear proteins MBP-1 (Baldwin et al., Mol. Cell. Biol. 10:1406-1414, 1990), PRDII-BFI (Fan and Maniatis, Genes Dev. 4:29-42, 1990), and HIV-EP1 (Maekawa et al., J. Biol. Chem. 264:14591-14593, 1989), which bind to regulatory elements of the MHC class I, beta interferon, and human immunodeficiency virus genes, respectively. Our results suggest that the lens-specific alpha A-crystallin, MHC class I, beta interferon and other genes have a similar cis-acting DNA regulatory motif that shares alpha A-CRYBPI, MBP-1, PRDII-BF1, HIV-EP1, or other closely related proteins as trans-acting factors.
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PMID:Regulation of the mouse alpha A-crystallin gene: isolation of a cDNA encoding a protein that binds to a cis sequence motif shared with the major histocompatibility complex class I gene and other genes. 169 16

At least two different types of proteins, NF-kappa B/KBF1 and HIV-EP1/PRDII-BF1/MBP-1, which are members of a family of rel oncoproteins and metal-finger proteins, respectively, bind to the human immunodeficiency virus type (HIV-1) enhancer. As a new member of a HIV-EP1 family that is expressed at a high level in T cells, we have isolated cDNA clones of HIV-EP2 by cross-hybridization with HIV-EP1 cDNA. HIV-EP2 protein consists of 1,833 amino acids and has a molecular weight of 211,000. HIV-EP2 protein is highly homologous with HIV-EP1/PRDII-BF1/MBP-1 in three regions. These three regions contain the potential nuclear localization signal followed by a Ser/Thr-rich region, the DNA-binding domain consisting of a metal-finger structure, and a cluster of acidic amino acids. The DNA-binding property of HIV-EP2 was similar to that of HIV-EP1. Northern blot analysis of HIV-EP2 mRNA indicated relatively high expression in the T cell line Molt-4 and in some tumor cell lines. Furthermore, like HIV-EP1, expression of HIV-EP2 mRNA was greatly induced by mitogen and phorbol ester treatment of Jurkat T cells, suggesting that HIV-EP2 acts in HIV production from latently infected T cells.
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PMID:HIV-EP2, a new member of the gene family encoding the human immunodeficiency virus type 1 enhancer-binding protein. Comparison with HIV-EP1/PRDII-BF1/MBP-1. 202 70

A variety of cellular proteins have been found to bind to related DNA sequences in the enhancer elements of the human immunodeficiency virus, the kappa immunoglobulin gene, the class I major histocompatibility complex gene, and the beta-interferon gene. Recently, lambda gt11 gene expression cloning using ligated oligonucleotide probes complementary to these DNA binding motifs has been performed. An identical cDNA clone encoding a cellular protein, referred to as HIV-EP1, MBP-1, or PRDII-BF1, that binds to each of these sequences has been identified. This cDNA potentially encodes a 298-kDa cellular protein with two widely separated zinc finger binding domains, each of which binds to the same DNA sequence. As part of an effort to examine the chromosomal organization of cellular genes encoding transcription factors, we report the chromosomal mapping of the gene encoding this zinc finger protein (ZNF40) to chromosome 6p22.3-24.
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PMID:Localization of the zinc finger DNA-binding protein HIV-EP1/MBP-1/PRDII-BF1 to human chromosome 6p22.3-p24. 203

Gene expression of human immunodeficiency virus (HIV) is modulated by both cellular transcription factors, which bind to cis-acting regulatory elements in the HIV-1 long terminal repeat (LTR) and the viral transactivator, tat. The enhancer element in the HIV-1 LTR which extends from -103 to -82 is critical for gene expression. This region contains two identical 10-bp direct repeats which serve as binding sites for members of the NF-kappa B family of transcription factors. However, several other cellular transcription factors, including a group of zinc finger DNA-binding proteins, also bind to NF-kappa B and related motifs. A member of this family of transcription factors, designated PRDII-BF1 or MBP-1, is a 300-kDa cellular protein which contains two widely separated zinc finger DNA binding domains. Each of these binding domains is capable of binding to NF-kappa B or related recognition motifs. Since no functional role for this protein has been demonstrated in the regulation of viral and cellular promoters, we began studies to determine whether PRDII-BF1 could modulate HIV-1 gene expression. DNase I footprinting of the HIV-1 LTR indicated that PRDII-BF1 bound to both NF-kappa B and TAR transactivation response DNA elements. Both in vitro translation and vaccinia virus expression of PRDII-BF1 cDNA resulted in the synthesis of the full-length 300-kDa PRDII-BF1 protein. Transfection experiments, using both eucaryotic expression vectors and antisense constructs, indicated that PRDII-BF1 activated HIV-1 gene expression in both the presence and absence of tat. These results are consistent with a role for PRDII-BF1 in activating HIV-1 gene expression.
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PMID:Transcription factor PRDII-BF1 activates human immunodeficiency virus type 1 gene expression. 828 30

A cellular transcriptional factor initially identified as the c-myc promoter binding protein (MBP-1) was subsequently characterized as a cell regulatory protein with multifunctional activities. In this study, the role of MBP-1 on human immunodeficiency virus type-1 (HIV-1) transcriptional activity was investigated. MBP-1 showed inhibition of HIV-1 long terminal repeat (LTR)-directed chloramphenicol acetyl transferase (CAT) activity in a transient cotransfection assay. Deletion of upstream elements of the HIV-1 LTR, including the nuclear factor kappa B (NF-kappa B) and Sp1 binding sites, did not affect the MBP-1 mediated suppression of HIV-1 LTR. The core promoter of the HIV-1 appeared to be the primary sequence involved in MBP-1 mediated inhibition. In the presence of HIV-1 TAR sequence and Tat protein, MBP-1 did not inhibit the viral promoter activity. In addition, cotransfection experiments with HIV-1 LTR and deletion mutants of MBP-1 suggested that the carboxyl terminal half of MBP-1 suppresses the HIV-1 promoter activity. Exogenous expression of MBP-1 showed suppression of HIV-1 replication in acutely infected cells and in cells cotransfected with a molecular clone of HIV-1. These results suggest that exogenous expression of MBP-1 plays an important role in the regulation of HIV-1 replication in infected cells.
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PMID:Inhibition of human immunodeficiency virus type 1 replication by a cellular transcriptional factor MBP-1. 909 5