Synthesis and sequence-specific DNA binding of a topoisomerase inhibitory analog of Hoechst 33258 designed for altered base and sequence recognition

1992 ◽  
Vol 5 (5) ◽  
pp. 597-607 ◽  
Author(s):  
Malvinder P. Singh ◽  
Tomi Joseph ◽  
Surat Kumar ◽  
Yadagiri Bathini ◽  
J. William Lown
Keyword(s):  
Dna Binding ◽  
Hoechst 33258 ◽  
Sequence Recognition

Pulse radiolysis of the DNA-binding bisbenzimidazole derivatives Hoechst 33258 and 33342 in aqueous solutions

2000 ◽  
Vol 76 (9) ◽  
pp. 1157-1166 ◽  
Author(s):  
A. Adhikary, E. Bothe, V. Jain, C. Von
Keyword(s):  
Dna Binding ◽  
Aqueous Solutions ◽  
Pulse Radiolysis ◽  
Hoechst 33258

scholarly journals Mechanism of DNA binding and sequence recognition by T7 DNA primase

2006 ◽  
Vol 20 (4) ◽  
Author(s):  
Seung‐Joo Lee ◽  
Samir M. Hamdan ◽  
Charles C. Richardson
Keyword(s):  
Dna Binding ◽  
Dna Primase ◽  
Sequence Recognition

scholarly journals E4F and ATF, two transcription factors that recognize the same site, can be distinguished both physically and functionally: a role for E4F in E1A trans activation.

1990 ◽  
Vol 10 (10) ◽  
pp. 5138-5149 ◽  
Author(s):  
R J Rooney ◽  
P Raychaudhuri ◽  
J R Nevins
Keyword(s):  
Dna Binding ◽  
Binding Activity ◽  
Stable Complex ◽  
Small Subset ◽  
Adenovirus Infection ◽  
Binding Assays ◽  
Dna Binding Activity ◽  
Sequence Recognition ◽  
Nuclear Factors ◽  
Dna Binding Factors

Previous experiments have identified an element in the adenovirus E4 promoter that is critical for E1A-dependent trans activation and that can confer inducibility to a heterologous promoter. This DNA element is a recognition site for multiple nuclear factors, including ATF, which is likely a family of DNA-binding factors with similar DNA recognition properties. However, ATF activity was found not to be altered in any demonstrable way as a result of adenovirus infection. In contrast, another factor that recognizes this element, termed E4F, was found at only very low levels in uninfected cells but was increased markedly upon adenovirus infection, as measured in DNA-binding assays. Although both the ATF activity and the E4F activity recognized and bound to the same two sites in the E4 promoter, they differed in their sequence recognition of these sites. Furthermore, E4F bound only to a small subset of the ATF recognition sites; for instance, E4F did not recognize the ATF sites in the E2 or E3 promoters. Various E4F and ATF binding sites were inserted into an expression vector and tested by cotransfection assays for responsiveness to E1A. We found that a sequence capable of binding E4F could confer E1A inducibility. In contrast, a sequence that could bind ATF but not E4F did not confer E1A inducibility. We also found that E4F formed a stable complex with the E4 promoter, whereas the ATF DNA complex was unstable and rapidly dissociated. We conclude that the DNA-binding specificity of E4F as well as the alterations in DNA-binding activity of E4F closely correlates with E1A stimulation of the E4 promoter.

scholarly journals Cooperative DNA-binding and sequence-recognition mechanism of aristaless and clawless

2010 ◽  
Vol 29 (9) ◽  
pp. 1613-1623 ◽  
Author(s):  
Ken-ichi Miyazono ◽  
Yuehua Zhi ◽  
Yuriko Takamura ◽  
Koji Nagata ◽  
Kaoru Saigo ◽  
...  
Keyword(s):  
Dna Binding ◽  
Recognition Mechanism ◽  
Sequence Recognition

DNA recognition by nuclear receptors

2004 ◽  
Vol 40 ◽  
pp. 59-72 ◽  
Author(s):  
Frank Claessens ◽  
Daniel T Gewirth
Keyword(s):  
Transcription Factors ◽  
Dna Binding ◽  
Nuclear Receptors ◽  
Dna Sequences ◽  
Dna Recognition ◽  
Binding Domain ◽  
Dna Binding Domain ◽  
Core Motif ◽  
Response Elements ◽  
Sequence Recognition

The nuclear receptors constitute a large family of ligand-inducible transcription factors. The control of many genetic pathways requires the assembly of these nuclear receptors in defined transcription-activating complexes within control regions of ligand-responsive genes. An essential step is the interaction of the receptors with specific DNA sequences, called hormone-response elements (HREs). These response elements position the receptors, and the complexes recruited by them, close to the genes of which transcription is affected. HREs are bipartite elements that are composed of two hexameric core half-site motifs. The identity of the response elements resides in three features: the nucleotide sequence of the two core motif half-sites, the number of base pairs separating them and the relative orientation of the motifs. The DNA-binding domains of nuclear receptors consist of two zinc-nucleated modules and a C-terminal extension. Residues in the first module determine the specificity of the DNA recognition, while residues in the second module are involved in dimerization. Indeed, nuclear receptors bind to their HREs as either homodimers or heterodimers. Depending on the type of receptor, the C-terminal extension plays a role in sequence recognition, dimerization, or both. The DNA-binding domain is furthermore involved in several other functions including nuclear localization, and interaction with transcription factors and co-activators. It is also the target of post-translational modifications. The DNA-binding domain therefore plays a central role, not only in the correct binding of the receptors to the target genes, but also in the control of other steps of the action mechanism of nuclear receptors.

scholarly journals Defining the sequence-recognition profile of DNA-binding molecules

2006 ◽  
Vol 103 (4) ◽  
pp. 867-872 ◽  
Author(s):  
C. L. Warren ◽  
N. C. S. Kratochvil ◽  
K. E. Hauschild ◽  
S. Foister ◽  
M. L. Brezinski ◽  
...  
Keyword(s):  
Dna Binding ◽  
Sequence Recognition
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