The Experts below are selected from a list of 282 Experts worldwide ranked by ideXlab platform
G. Geoff Kneale - One of the best experts on this subject based on the ideXlab platform.
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Single stranded DNA-Binding proteins
Current Opinion in Structural Biology, 1992Co-Authors: G. Geoff KnealeAbstract:Abstract The past year has seen steady progress in our understanding of single stranded DNA-Binding proteins and their interaction with DNA, most notably of the gene 5 proteins of bacteriophages fd and Pf, the gene 32 protein of bacteriophage T4 and the Escherichia coli SSB protein. A brief survey is given of recently identified single stranded DNA-Binding proteins from both prokaryotic and eukaryotic sources, a number of which show pronounced sequence specificity. The crystal structure of the E. coli recA protein, which binds to both single-stranded and duplex DNA, has very recently been reported, and is briefly discussed.
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Single stranded DNA-Binding proteins
Current Opinion in Structural Biology, 1992Co-Authors: G. Geoff KnealeAbstract:Abstract The past year has seen steady progress in our understanding of single stranded DNA-Binding proteins and their interaction with DNA, most notably of the gene 5 proteins of bacteriophages fd and Pf, the gene 32 protein of bacteriophage T4 and the Escherichia coli SSB protein. A brief survey is given of recently identified single stranded DNA-Binding proteins from both prokaryotic and eukaryotic sources, a number of which show pronounced sequence specificity. The crystal structure of the E. coli recA protein, which binds to both single-stranded and duplex DNA, has very recently been reported, and is briefly discussed.
Di Liu - One of the best experts on this subject based on the ideXlab platform.
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Single-stranded DNA-Binding proteins in plant telomeres.
International journal of biological macromolecules, 2020Co-Authors: Mei Luo, Heng Luo, Di LiuAbstract:Abstract Telomere single-stranded DNA-Binding proteins bind to the terminal single-stranded DNA of telomeres, maintaining and protecting the chromosomal end in eukaryotes. This paper focuses on the protective mechanism of single-stranded DNA-Binding proteins in plant telomeres. This review summarizes the roles of plant single-stranded DNA-Binding proteins and their influence on telomere length and telomerase. This review provides insights into the mechanism and development of single-stranded DNA-Binding proteins in plants.
Jan Carlstedt-duke - One of the best experts on this subject based on the ideXlab platform.
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Protein-protein interactions between the DNA-Binding domains of nuclear receptors: Influence on DNA-Binding
The Journal of steroid biochemistry and molecular biology, 1993Co-Authors: Karin Dahlman-wright, Kaj Grandien, Stefan K. Nilsson, Jan-ake Gustafsson, Jan Carlstedt-dukeAbstract:The glucocorticoid and thyroid hormone receptors have the capacity to bind as dimers to palindromic DNA-Binding sites. Protein-protein interactions between the DNA-Binding domains of glucocorticoid receptor dimers restrict the DNA-Binding to elements where the half-sites are separated by three base pairs, whereas DNA-Binding by the thyroid hormone receptor does not appear to require a strict half-site spacing. We have previously shown that a five amino-acid segment close the the C-terminal zinc-Binding site (D-box) was involved in dimerization of the glucocorticoid receptor (GR) DNA-Binding domain (Dahlman-Wright et al., 1991, J. Biol. Chem., 266, 3107–3112). Here we provide functional evidence, using mutated thyroid hormone receptor DNA-Binding domains, that this five amino acid segment (D-box) of the GR interacts with the equivalent segment on the second DNA-Binding domain in the dimer. In contrast, the thyroid hormone receptor DNA-Binding domain binds to palindromic thyroid hormone response elements in a weakly co-operative manner, independent of the D-box.
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DNA Binding specificity of mutant glucocorticoid receptor DNA-Binding domains.
The Journal of biological chemistry, 1991Co-Authors: Johanna Zilliacus, Karin Dahlman-wright, Jan-ake Gustafsson, Anthony P. H. Wright, Jan Carlstedt-dukeAbstract:Abstract Mutation of a small number of amino acids in the DNA-Binding domain of the estrogen receptor to the corresponding sequence of the glucocorticoid receptor switches the specificity of the receptor in transactivation assays (Mader, S., Kumar, V., de Verneuil, H., and Chambon, P. (1989) Nature 338, 271-274). We have made the corresponding reciprocal mutations in the context of the glucocorticoid receptor DNA-Binding domain and studied the Binding of wild type and mutant purified proteins to palindromic glucocorticoid and estrogen response elements as well as to elements of intermediate sequence, using gel mobility shift assays. We show here that a protein with two altered amino acids binds glucocorticoid and estrogen response elements with a low but equal affinity, whereas a protein with an additional changed residue has a high affinity for estrogen response elements but still retains a considerable affinity for glucocorticoid response elements. Using Binding sites of intermediate sequence we have further characterized the interaction with DNA. The in vitro DNA Binding results are confirmed by in vivo transactivation assays in yeast. Finally we suggest a testable model for amino acid/base pair interactions involved in recognition by the glucocorticoid receptor DNA-Binding domain of its target sequence.
Lori Frappier - One of the best experts on this subject based on the ideXlab platform.
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Two Domains of the Epstein-Barr Virus Origin DNA-Binding Protein, EBNA1, Orchestrate Sequence-specific DNA Binding
The Journal of biological chemistry, 2000Co-Authors: Jennifer Cruickshank, Aled M Edwards, Kathy Shire, Alan R. Davidson, Lori FrappierAbstract:The EBNA1 (for Epstein-Barr nuclear antigen 1) protein of Epstein-Barr virus governs the replication and partitioning of the viral genomes during latent infection by Binding to specific recognition sites in the viral origin of DNA replication. The crystal structure of the DNA Binding portion of the EBNA1 protein revealed that this region comprises two structural motifs; a core domain, which mediates protein dimerization and is structurally homologous to the DNA Binding domain of the papillomavirus E2 protein, and a flanking domain, which mediated all the observed sequence-specific contacts. To test the possibility that the EBNA1 core domain plays a role in sequence-specific DNA Binding not revealed in the crystal structure, we examined the effects of point mutations in potential hydrogen bond donors located in an alpha-helix of the EBNA1 core domain whose structural homologue in E2 mediates sequence-specific DNA Binding. We show that these mutations severely reduce the affinity of EBNA1 for its recognition site, and that the core domain, when expressed in the absence of the flanking domain, has sequence-specific DNA Binding activity. Flanking domain residues were also found to contribute to the DNA Binding activity of EBNA1. Thus, both the core and flanking domains of EBNA1 play direct roles in DNA recognition.
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Origin DNA-Binding proteins
Current Opinion in Structural Biology, 1998Co-Authors: Aled M Edwards, A Bochkarev, Lori FrappierAbstract:Abstract The first step in DNA replication involves the recognition of origin DNA sequences by origin-Binding proteins. The three-dimensional structures of three different origin DNA-Binding proteins have recently been solved. These proteins form a structural class distinct from other DNA-Binding proteins. One of the origin-Binding proteins, Epstein—Barr virus nuclear antigen 1, most likely has two modes of DNA Binding; the sequential use of these modes may be important for the initiation of DNA replication.
Karin Dahlman-wright - One of the best experts on this subject based on the ideXlab platform.
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Protein-protein interactions between the DNA-Binding domains of nuclear receptors: Influence on DNA-Binding
The Journal of steroid biochemistry and molecular biology, 1993Co-Authors: Karin Dahlman-wright, Kaj Grandien, Stefan K. Nilsson, Jan-ake Gustafsson, Jan Carlstedt-dukeAbstract:The glucocorticoid and thyroid hormone receptors have the capacity to bind as dimers to palindromic DNA-Binding sites. Protein-protein interactions between the DNA-Binding domains of glucocorticoid receptor dimers restrict the DNA-Binding to elements where the half-sites are separated by three base pairs, whereas DNA-Binding by the thyroid hormone receptor does not appear to require a strict half-site spacing. We have previously shown that a five amino-acid segment close the the C-terminal zinc-Binding site (D-box) was involved in dimerization of the glucocorticoid receptor (GR) DNA-Binding domain (Dahlman-Wright et al., 1991, J. Biol. Chem., 266, 3107–3112). Here we provide functional evidence, using mutated thyroid hormone receptor DNA-Binding domains, that this five amino acid segment (D-box) of the GR interacts with the equivalent segment on the second DNA-Binding domain in the dimer. In contrast, the thyroid hormone receptor DNA-Binding domain binds to palindromic thyroid hormone response elements in a weakly co-operative manner, independent of the D-box.
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Determinants of high-affinity DNA Binding by the glucocorticoid receptor: Evaluation of receptor domains outside the DNA-Binding domain
Biochemistry, 1992Co-Authors: Karin Dahlman-wright, Anthony P. H. Wright, Jan Aake GustafssonAbstract:In this study, we have investigated the influence of regions outside the DNA-Binding domain of the human glucocorticoid receptor on high-affinity DNA Binding. We find that the DNA-Binding domain shows a 10-fold lower affinity for a palindromic DNA-Binding site than the intact receptor. The N-terminal part of the receptor protein does not influence its DNA-Binding affinity, while the C-terminal steroid-Binding domain increases the DNA-Binding affinity of the receptor molecule. It has previously been shown that both the intact glucocorticoid receptor and the glucocorticoid receptor DNA-Binding domain bind to a palindromic glucocorticoid response element on DNA as dimers. It is likely that differences in DNA-Binding affinity observed result from protein-protein interactions outside the DNA-Binding domain between receptor monomers, as has been shown for the estrogen receptor. We have previously identified a segment involved in protein-protein interactions between DNA-Binding domains of glucocorticoid receptors. This, in combination with results presented in this study, suggests that there are at least two sites of contact between receptor monomers bound to DNA. We suggest that the interaction between the DNA-Binding domains may act primarily to restrict DNA Binding to Binding sites with appropriate half-site spacing and that additional stability of the receptor dimer is provided by the interactions between the steroid-Binding domains.
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DNA Binding specificity of mutant glucocorticoid receptor DNA-Binding domains.
The Journal of biological chemistry, 1991Co-Authors: Johanna Zilliacus, Karin Dahlman-wright, Jan-ake Gustafsson, Anthony P. H. Wright, Jan Carlstedt-dukeAbstract:Abstract Mutation of a small number of amino acids in the DNA-Binding domain of the estrogen receptor to the corresponding sequence of the glucocorticoid receptor switches the specificity of the receptor in transactivation assays (Mader, S., Kumar, V., de Verneuil, H., and Chambon, P. (1989) Nature 338, 271-274). We have made the corresponding reciprocal mutations in the context of the glucocorticoid receptor DNA-Binding domain and studied the Binding of wild type and mutant purified proteins to palindromic glucocorticoid and estrogen response elements as well as to elements of intermediate sequence, using gel mobility shift assays. We show here that a protein with two altered amino acids binds glucocorticoid and estrogen response elements with a low but equal affinity, whereas a protein with an additional changed residue has a high affinity for estrogen response elements but still retains a considerable affinity for glucocorticoid response elements. Using Binding sites of intermediate sequence we have further characterized the interaction with DNA. The in vitro DNA Binding results are confirmed by in vivo transactivation assays in yeast. Finally we suggest a testable model for amino acid/base pair interactions involved in recognition by the glucocorticoid receptor DNA-Binding domain of its target sequence.
