The Experts below are selected from a list of 20196 Experts worldwide ranked by ideXlab platform
Reinhard Kurth - One of the best experts on this subject based on the ideXlab platform.
-
ga binding protein factors in concert with the coactivator creb binding protein p300 control the induction of the interleukin 16 promoter in t lymphocytes
Proceedings of the National Academy of Sciences of the United States of America, 1999Co-Authors: Norbert Bannert, Michael Baier, Andris Avots, Edgar Serfling, Reinhard KurthAbstract:Interleukin 16 (IL-16) is a chemotactic cytokine that binds to the CD4 receptor and affects the activation of T cells and replication of HIV. It is expressed as a large 67-kDa precursor protein (pro-IL-16) in lymphocytes, macrophages, and mast cells, as well as in airway epithelial cells from asthmatics after challenge with allergen. This pro-IL-16 is subsequently processed to the mature cytokine of 13 kDa. To study the expression of IL-16 at the transcriptional level, we cloned the human chromosomal IL-16 gene and analyzed its promoter. The human IL-16 gene consists of seven exons and six introns. The 5′ sequences up to nucleotide −120 of the human and murine IL-16 genes share >84% sequence homology and harbor promoter Elements for constitutive and inducible transcription in T cells. Although both promoters lack any TATA box, they contain two CAAT box-like motifs and three binding sites of GA-binding protein (GABP) transcription factors. Two of these motifs are part of a highly conserved and inducible dyad Symmetry Element shown previously to control a remote IL-2 enhancer and the CD18 promoter. In concert with the coactivator CREB binding protein/p300, which interacts with GABPα, the binding of GABPα and -β to the dyad Symmetry Element controls the induction of IL-16 promoter in T cells. Supplementing the data on the processing of pro-IL-16, our results indicate the complexity of IL-16 expression, which is tightly controlled at the transcriptional and posttranslational levels in T lymphocytes.
-
GA-binding protein factors, in concert with the coactivator CREB binding protein/p300, control the induction of the interleukin 16 promoter in T lymphocytes.
Proceedings of the National Academy of Sciences of the United States of America, 1999Co-Authors: Norbert Bannert, Michael Baier, Andris Avots, Edgar Serfling, Reinhard KurthAbstract:Interleukin 16 (IL-16) is a chemotactic cytokine that binds to the CD4 receptor and affects the activation of T cells and replication of HIV. It is expressed as a large 67-kDa precursor protein (pro-IL-16) in lymphocytes, macrophages, and mast cells, as well as in airway epithelial cells from asthmatics after challenge with allergen. This pro-IL-16 is subsequently processed to the mature cytokine of 13 kDa. To study the expression of IL-16 at the transcriptional level, we cloned the human chromosomal IL-16 gene and analyzed its promoter. The human IL-16 gene consists of seven exons and six introns. The 5′ sequences up to nucleotide −120 of the human and murine IL-16 genes share >84% sequence homology and harbor promoter Elements for constitutive and inducible transcription in T cells. Although both promoters lack any TATA box, they contain two CAAT box-like motifs and three binding sites of GA-binding protein (GABP) transcription factors. Two of these motifs are part of a highly conserved and inducible dyad Symmetry Element shown previously to control a remote IL-2 enhancer and the CD18 promoter. In concert with the coactivator CREB binding protein/p300, which interacts with GABPα, the binding of GABPα and -β to the dyad Symmetry Element controls the induction of IL-16 promoter in T cells. Supplementing the data on the processing of pro-IL-16, our results indicate the complexity of IL-16 expression, which is tightly controlled at the transcriptional and posttranslational levels in T lymphocytes.
Hisao Masai - One of the best experts on this subject based on the ideXlab platform.
-
epstein barr nuclear antigen 1 ebna1 dependent recruitment of origin recognition complex orc on orip of epstein barr virus with purified proteins stimulation by cdc6 through its direct interaction with ebna1
Journal of Biological Chemistry, 2012Co-Authors: Kenji Moriyama, Naoko Yoshizawasugata, Chikashi Obuse, Toshiki Tsurimoto, Hisao MasaiAbstract:Abstract Origin recognition complex (Orc) plays an essential role in directing assembly of prereplicative complex at selective sites on chromosomes. However, Orc from vertebrates is reported to bind to DNA in a sequence-nonspecific manner, and it is still unclear how it selects specific genomic loci and how Cdc6, another conserved AAA+ factor known to interact with Orc, participates in this process. Replication from oriP, the latent origin of Epstein-Barr virus, provides an excellent model system for the study of initiation on the host chromosomes because it is known to depend on prereplicative complex factors, including Orc and Mcm. Here, we show that Orc is recruited selectively at the essential dyad Symmetry Element in nuclear extracts in a manner dependent on EBNA1, which specifically binds to dyad Symmetry. With purified proteins, EBNA1 can recruit both Cdc6 and Orc independently on a DNA containing EBNA1 binding sites, and Cdc6 facilitates the Orc recruitment by EBNA1. Purified Cdc6 directly binds to EBNA1, whereas association of Orc with EBNA1 requires the presence of the oriP DNA. Nuclease protection assays suggest that Orc associates with DNA segments on both sides adjacent to the EBNA1 binding sites and that this process is stimulated by the presence of Cdc6. Thus, EBNA1 can direct localized assembly of Orc in a process that is facilitated by Cdc6. The possibility of similar modes of recruitment of Orc/Cdc6 at the human chromosomal origins will be discussed.
-
epstein barr nuclear antigen 1 ebna1 dependent recruitment of origin recognition complex orc on orip of epstein barr virus with purified proteins stimulation by cdc6 through its direct interaction with ebna1
Journal of Biological Chemistry, 2012Co-Authors: Kenji Moriyama, Naoko Yoshizawasugata, Chikashi Obuse, Toshiki Tsurimoto, Hisao MasaiAbstract:Origin recognition complex (Orc) plays an essential role in directing assembly of prereplicative complex at selective sites on chromosomes. However, Orc from vertebrates is reported to bind to DNA in a sequence-nonspecific manner, and it is still unclear how it selects specific genomic loci and how Cdc6, another conserved AAA+ factor known to interact with Orc, participates in this process. Replication from oriP, the latent origin of Epstein-Barr virus, provides an excellent model system for the study of initiation on the host chromosomes because it is known to depend on prereplicative complex factors, including Orc and Mcm. Here, we show that Orc is recruited selectively at the essential dyad Symmetry Element in nuclear extracts in a manner dependent on EBNA1, which specifically binds to dyad Symmetry. With purified proteins, EBNA1 can recruit both Cdc6 and Orc independently on a DNA containing EBNA1 binding sites, and Cdc6 facilitates the Orc recruitment by EBNA1. Purified Cdc6 directly binds to EBNA1, whereas association of Orc with EBNA1 requires the presence of the oriP DNA. Nuclease protection assays suggest that Orc associates with DNA segments on both sides adjacent to the EBNA1 binding sites and that this process is stimulated by the presence of Cdc6. Thus, EBNA1 can direct localized assembly of Orc in a process that is facilitated by Cdc6. The possibility of similar modes of recruitment of Orc/Cdc6 at the human chromosomal origins will be discussed. Background: Enzymatic studies on the steps of mammalian DNA replication with purified proteins are essential to elucidate its mechanisms. Results: Association of Orc with oriP requires EBNA1 and is stimulated by Cdc6 directly interacting with EBNA1. Conclusion: EBNA1 recruits Cdc6/Orc at oriP, permitting site-specific assembly of pre-RC. Significance: This study provides novel insight into a mechanism for initiation of mammalian DNA replication with purified factors.
Norbert Bannert - One of the best experts on this subject based on the ideXlab platform.
-
ga binding protein factors in concert with the coactivator creb binding protein p300 control the induction of the interleukin 16 promoter in t lymphocytes
Proceedings of the National Academy of Sciences of the United States of America, 1999Co-Authors: Norbert Bannert, Michael Baier, Andris Avots, Edgar Serfling, Reinhard KurthAbstract:Interleukin 16 (IL-16) is a chemotactic cytokine that binds to the CD4 receptor and affects the activation of T cells and replication of HIV. It is expressed as a large 67-kDa precursor protein (pro-IL-16) in lymphocytes, macrophages, and mast cells, as well as in airway epithelial cells from asthmatics after challenge with allergen. This pro-IL-16 is subsequently processed to the mature cytokine of 13 kDa. To study the expression of IL-16 at the transcriptional level, we cloned the human chromosomal IL-16 gene and analyzed its promoter. The human IL-16 gene consists of seven exons and six introns. The 5′ sequences up to nucleotide −120 of the human and murine IL-16 genes share >84% sequence homology and harbor promoter Elements for constitutive and inducible transcription in T cells. Although both promoters lack any TATA box, they contain two CAAT box-like motifs and three binding sites of GA-binding protein (GABP) transcription factors. Two of these motifs are part of a highly conserved and inducible dyad Symmetry Element shown previously to control a remote IL-2 enhancer and the CD18 promoter. In concert with the coactivator CREB binding protein/p300, which interacts with GABPα, the binding of GABPα and -β to the dyad Symmetry Element controls the induction of IL-16 promoter in T cells. Supplementing the data on the processing of pro-IL-16, our results indicate the complexity of IL-16 expression, which is tightly controlled at the transcriptional and posttranslational levels in T lymphocytes.
-
GA-binding protein factors, in concert with the coactivator CREB binding protein/p300, control the induction of the interleukin 16 promoter in T lymphocytes.
Proceedings of the National Academy of Sciences of the United States of America, 1999Co-Authors: Norbert Bannert, Michael Baier, Andris Avots, Edgar Serfling, Reinhard KurthAbstract:Interleukin 16 (IL-16) is a chemotactic cytokine that binds to the CD4 receptor and affects the activation of T cells and replication of HIV. It is expressed as a large 67-kDa precursor protein (pro-IL-16) in lymphocytes, macrophages, and mast cells, as well as in airway epithelial cells from asthmatics after challenge with allergen. This pro-IL-16 is subsequently processed to the mature cytokine of 13 kDa. To study the expression of IL-16 at the transcriptional level, we cloned the human chromosomal IL-16 gene and analyzed its promoter. The human IL-16 gene consists of seven exons and six introns. The 5′ sequences up to nucleotide −120 of the human and murine IL-16 genes share >84% sequence homology and harbor promoter Elements for constitutive and inducible transcription in T cells. Although both promoters lack any TATA box, they contain two CAAT box-like motifs and three binding sites of GA-binding protein (GABP) transcription factors. Two of these motifs are part of a highly conserved and inducible dyad Symmetry Element shown previously to control a remote IL-2 enhancer and the CD18 promoter. In concert with the coactivator CREB binding protein/p300, which interacts with GABPα, the binding of GABPα and -β to the dyad Symmetry Element controls the induction of IL-16 promoter in T cells. Supplementing the data on the processing of pro-IL-16, our results indicate the complexity of IL-16 expression, which is tightly controlled at the transcriptional and posttranslational levels in T lymphocytes.
Kenji Moriyama - One of the best experts on this subject based on the ideXlab platform.
-
epstein barr nuclear antigen 1 ebna1 dependent recruitment of origin recognition complex orc on orip of epstein barr virus with purified proteins stimulation by cdc6 through its direct interaction with ebna1
Journal of Biological Chemistry, 2012Co-Authors: Kenji Moriyama, Naoko Yoshizawasugata, Chikashi Obuse, Toshiki Tsurimoto, Hisao MasaiAbstract:Abstract Origin recognition complex (Orc) plays an essential role in directing assembly of prereplicative complex at selective sites on chromosomes. However, Orc from vertebrates is reported to bind to DNA in a sequence-nonspecific manner, and it is still unclear how it selects specific genomic loci and how Cdc6, another conserved AAA+ factor known to interact with Orc, participates in this process. Replication from oriP, the latent origin of Epstein-Barr virus, provides an excellent model system for the study of initiation on the host chromosomes because it is known to depend on prereplicative complex factors, including Orc and Mcm. Here, we show that Orc is recruited selectively at the essential dyad Symmetry Element in nuclear extracts in a manner dependent on EBNA1, which specifically binds to dyad Symmetry. With purified proteins, EBNA1 can recruit both Cdc6 and Orc independently on a DNA containing EBNA1 binding sites, and Cdc6 facilitates the Orc recruitment by EBNA1. Purified Cdc6 directly binds to EBNA1, whereas association of Orc with EBNA1 requires the presence of the oriP DNA. Nuclease protection assays suggest that Orc associates with DNA segments on both sides adjacent to the EBNA1 binding sites and that this process is stimulated by the presence of Cdc6. Thus, EBNA1 can direct localized assembly of Orc in a process that is facilitated by Cdc6. The possibility of similar modes of recruitment of Orc/Cdc6 at the human chromosomal origins will be discussed.
-
epstein barr nuclear antigen 1 ebna1 dependent recruitment of origin recognition complex orc on orip of epstein barr virus with purified proteins stimulation by cdc6 through its direct interaction with ebna1
Journal of Biological Chemistry, 2012Co-Authors: Kenji Moriyama, Naoko Yoshizawasugata, Chikashi Obuse, Toshiki Tsurimoto, Hisao MasaiAbstract:Origin recognition complex (Orc) plays an essential role in directing assembly of prereplicative complex at selective sites on chromosomes. However, Orc from vertebrates is reported to bind to DNA in a sequence-nonspecific manner, and it is still unclear how it selects specific genomic loci and how Cdc6, another conserved AAA+ factor known to interact with Orc, participates in this process. Replication from oriP, the latent origin of Epstein-Barr virus, provides an excellent model system for the study of initiation on the host chromosomes because it is known to depend on prereplicative complex factors, including Orc and Mcm. Here, we show that Orc is recruited selectively at the essential dyad Symmetry Element in nuclear extracts in a manner dependent on EBNA1, which specifically binds to dyad Symmetry. With purified proteins, EBNA1 can recruit both Cdc6 and Orc independently on a DNA containing EBNA1 binding sites, and Cdc6 facilitates the Orc recruitment by EBNA1. Purified Cdc6 directly binds to EBNA1, whereas association of Orc with EBNA1 requires the presence of the oriP DNA. Nuclease protection assays suggest that Orc associates with DNA segments on both sides adjacent to the EBNA1 binding sites and that this process is stimulated by the presence of Cdc6. Thus, EBNA1 can direct localized assembly of Orc in a process that is facilitated by Cdc6. The possibility of similar modes of recruitment of Orc/Cdc6 at the human chromosomal origins will be discussed. Background: Enzymatic studies on the steps of mammalian DNA replication with purified proteins are essential to elucidate its mechanisms. Results: Association of Orc with oriP requires EBNA1 and is stimulated by Cdc6 directly interacting with EBNA1. Conclusion: EBNA1 recruits Cdc6/Orc at oriP, permitting site-specific assembly of pre-RC. Significance: This study provides novel insight into a mechanism for initiation of mammalian DNA replication with purified factors.
Edgar Serfling - One of the best experts on this subject based on the ideXlab platform.
-
ga binding protein factors in concert with the coactivator creb binding protein p300 control the induction of the interleukin 16 promoter in t lymphocytes
Proceedings of the National Academy of Sciences of the United States of America, 1999Co-Authors: Norbert Bannert, Michael Baier, Andris Avots, Edgar Serfling, Reinhard KurthAbstract:Interleukin 16 (IL-16) is a chemotactic cytokine that binds to the CD4 receptor and affects the activation of T cells and replication of HIV. It is expressed as a large 67-kDa precursor protein (pro-IL-16) in lymphocytes, macrophages, and mast cells, as well as in airway epithelial cells from asthmatics after challenge with allergen. This pro-IL-16 is subsequently processed to the mature cytokine of 13 kDa. To study the expression of IL-16 at the transcriptional level, we cloned the human chromosomal IL-16 gene and analyzed its promoter. The human IL-16 gene consists of seven exons and six introns. The 5′ sequences up to nucleotide −120 of the human and murine IL-16 genes share >84% sequence homology and harbor promoter Elements for constitutive and inducible transcription in T cells. Although both promoters lack any TATA box, they contain two CAAT box-like motifs and three binding sites of GA-binding protein (GABP) transcription factors. Two of these motifs are part of a highly conserved and inducible dyad Symmetry Element shown previously to control a remote IL-2 enhancer and the CD18 promoter. In concert with the coactivator CREB binding protein/p300, which interacts with GABPα, the binding of GABPα and -β to the dyad Symmetry Element controls the induction of IL-16 promoter in T cells. Supplementing the data on the processing of pro-IL-16, our results indicate the complexity of IL-16 expression, which is tightly controlled at the transcriptional and posttranslational levels in T lymphocytes.
-
GA-binding protein factors, in concert with the coactivator CREB binding protein/p300, control the induction of the interleukin 16 promoter in T lymphocytes.
Proceedings of the National Academy of Sciences of the United States of America, 1999Co-Authors: Norbert Bannert, Michael Baier, Andris Avots, Edgar Serfling, Reinhard KurthAbstract:Interleukin 16 (IL-16) is a chemotactic cytokine that binds to the CD4 receptor and affects the activation of T cells and replication of HIV. It is expressed as a large 67-kDa precursor protein (pro-IL-16) in lymphocytes, macrophages, and mast cells, as well as in airway epithelial cells from asthmatics after challenge with allergen. This pro-IL-16 is subsequently processed to the mature cytokine of 13 kDa. To study the expression of IL-16 at the transcriptional level, we cloned the human chromosomal IL-16 gene and analyzed its promoter. The human IL-16 gene consists of seven exons and six introns. The 5′ sequences up to nucleotide −120 of the human and murine IL-16 genes share >84% sequence homology and harbor promoter Elements for constitutive and inducible transcription in T cells. Although both promoters lack any TATA box, they contain two CAAT box-like motifs and three binding sites of GA-binding protein (GABP) transcription factors. Two of these motifs are part of a highly conserved and inducible dyad Symmetry Element shown previously to control a remote IL-2 enhancer and the CD18 promoter. In concert with the coactivator CREB binding protein/p300, which interacts with GABPα, the binding of GABPα and -β to the dyad Symmetry Element controls the induction of IL-16 promoter in T cells. Supplementing the data on the processing of pro-IL-16, our results indicate the complexity of IL-16 expression, which is tightly controlled at the transcriptional and posttranslational levels in T lymphocytes.
