Isolation of a library of target-sites for sequence specific DNA binding proteins from chick embryonic heart: a potential tool for identifying novel transcriptional regulators involved in embryonic development

2004 ◽  
Vol 323 (3) ◽  
pp. 912-919 ◽  
Author(s):  
K.V. Sindhu ◽  
Vibha Rani ◽  
Manveen K. Gupta ◽  
Surendra Ghaskadbi ◽  
Devapriya Choudhury ◽  
...  
Keyword(s):  
Dna Binding ◽  
Embryonic Development ◽  
Binding Proteins ◽  
Transcriptional Regulators ◽  
Dna Binding Proteins ◽  
Embryonic Heart ◽  
Target Sites ◽  
Potential Tool

South Western blot mapping: A procedure for simultaneous characterization of DNA binding proteins and their specific genomic DNA target sites

1989 ◽  
Vol 179 (2) ◽  
pp. 299-303 ◽  
Author(s):  
Jean-Claude Lelong ◽  
Grégoire Prevost ◽  
Kyong il Lee ◽  
Michel Crepin
Keyword(s):  
Dna Binding ◽  
Western Blot ◽  
Genomic Dna ◽  
Binding Proteins ◽  
Dna Binding Proteins ◽  
Target Sites

scholarly journals How DNA-Binding Proteins find their Target Sites in Human Cells

2013 ◽  
Vol 104 (2) ◽  
pp. 541a-542a
Author(s):  
Davide Normanno ◽  
Lydia Boudaréne ◽  
Claire Dugast-Darzacq ◽  
Xavier Darzacq ◽  
Maxime Dahan
Keyword(s):  
Dna Binding ◽  
Binding Proteins ◽  
Dna Binding Proteins ◽  
Human Cells ◽  
Target Sites

scholarly journals Collaborative Competition Mechanism for Gene Activation In Vivo

2003 ◽  
Vol 23 (5) ◽  
pp. 1623-1632 ◽  
Author(s):  
Joanna A. Miller ◽  
Jonathan Widom
Keyword(s):  
Dna Binding ◽  
Binding Proteins ◽  
Regulatory Protein ◽  
Gene Activation ◽  
Dna Binding Proteins ◽  
Regulatory Proteins ◽  
Target Sites ◽  
Collaborative Competition

ABSTRACT The mechanism by which gene regulatory proteins gain access to their DNA target sites is not known. In vitro, binding is inherently cooperative between arbitrary DNA binding proteins whose target sites are located within the same nucleosome. We refer to such competition-based cooperativity as collaborative competition. Here we show that arbitrarily chosen foreign DNA binding proteins, LexA and Tet repressor, cooperate with an adjacently binding endogenous activator protein, Gcn4, to coactivate expression of chromosomal reporter genes in Saccharomyces cerevisiae. Coactivation requires that the cooperating target sites be within a nucleosome-length distance; it leads to increased occupancy by Gcn4 at its binding site; and it requires both Gcn5 and Swi/Snf which, at an endogenous Gcn4-dependent promoter, act subsequent to Gcn4 binding. These results imply that collaborative competition contributes to gene regulation in vivo. They further imply that, even in the presence of the cell's full wild-type complement of chromatin remodeling factors, competition of regulatory proteins with histone octamer for access to regulatory target sites remains a quantitative determinant of gene expression levels. We speculate that initial target site recognition and binding may occur via spontaneous nucleosomal site exposure, with remodeling factor action required downstream to lock in higher levels of regulatory protein occupancy.

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