scholarly journals Determining DNA Sequence Specificity of Natural and Artificial Transcription Factors by Cognate Site Identifier Analysis

Author(s):  
Mary S. Ozers ◽  
Christopher L. Warren ◽  
Aseem Z. Ansari
1987 ◽  
Vol 262 (18) ◽  
pp. 8868-8874 ◽  
Author(s):  
M Fry ◽  
R Sharf ◽  
P Weisman-Shomer ◽  
P C Evers ◽  
L A Loeb

1991 ◽  
Vol 11 (3) ◽  
pp. 1686-1695 ◽  
Author(s):  
M K Shivji ◽  
N B La Thangue

Murine F9 embryonal carcinoma (F9 EC) stem cells have an E1a-like transcription activity that is down-regulated as these cells differentiate to parietal endoderm. For the adenovirus E2A promoter, this activity requires at least two sequence-specific transcription factors, one that binds the cyclic AMP-responsive element (CRE) and the other, DRTF1, the DNA-binding activity of which is down-regulated as F9 EC cells differentiate. Here we report the characterization of several binding activities in F9 EC cell extracts, referred to as DRTF 1a, 1b and 1c, that recognize the DRTF1 cis-regulatory sequence (-70 to -50 region). These activities can be chromatographically separated but are not distinguishable by DNA sequence specificity. Activity 1a is a detergent-sensitive complex in which DNA binding is regulated by phosphorylation. In contrast, activities 1b and 1c are unaffected by these treatments but exist as multicomponent protein complexes even before DNA binding. Two sets of DNA-binding polypeptides, p50DR and p30DR, affinity purified from F9 EC cell extracts produce complexes 1b and 1c. Both polypeptides appear to be present in the same DNA-bound protein complex and both directly contact DNA. These affinity-purified polypeptides activate transcription in vitro in a binding-site-dependent manner. These data indicate the in F9 EC stem cells, multicomponent differentiation-regulated transcription factors contribute to the cellular E1a-like activity.


2005 ◽  
Vol 348 (2) ◽  
pp. 307-324 ◽  
Author(s):  
Paul J. Sapienza ◽  
Crystal A. dela Torre ◽  
William H. McCoy ◽  
Samyukta V. Jana ◽  
Linda Jen-Jacobson

Science ◽  
1984 ◽  
Vol 226 (4676) ◽  
pp. 843-844 ◽  
Author(s):  
L. Hurley ◽  
V. Reynolds ◽  
D. Swenson ◽  
G. Petzold ◽  
T. Scahill

1989 ◽  
Vol 9 (3) ◽  
pp. 1351-1356 ◽  
Author(s):  
D L Zhang ◽  
K C Ehrlich ◽  
P C Supakar ◽  
M Ehrlich

A novel, 5-methylcytosine-specific, DNA-binding protein, DBP-m, has been identified in nuclear extracts of peas. DBP-m specifically recognizes 5-methylcytosine residues in DNA without appreciable DNA sequence specificity, unlike a mammalian DNA-binding protein (MDBP), which recognizes 5-methylcytosine residues but only in a related family of 14-base-pair sequences.


2020 ◽  
Vol 11 (1) ◽  
Author(s):  
Y. Hu ◽  
A. Tareen ◽  
Y-J. Sheu ◽  
W. T. Ireland ◽  
C. Speck ◽  
...  

Abstract DNA replication in eukaryotic cells initiates from replication origins that bind the Origin Recognition Complex (ORC). Origin establishment requires well-defined DNA sequence motifs in Saccharomyces cerevisiae and some other budding yeasts, but most eukaryotes lack sequence-specific origins. A 3.9 Å structure of S. cerevisiae ORC-Cdc6-Cdt1-Mcm2-7 (OCCM) bound to origin DNA revealed that a loop within Orc2 inserts into a DNA minor groove and an α-helix within Orc4 inserts into a DNA major groove. Using a massively parallel origin selection assay coupled with a custom mutual-information-based modeling approach, and a separate analysis of whole-genome replication profiling, here we show that the Orc4 α-helix contributes to the DNA sequence-specificity of origins in S. cerevisiae and Orc4 α-helix mutations change genome-wide origin firing patterns. The DNA sequence specificity of replication origins, mediated by the Orc4 α-helix, has co-evolved with the gain of ORC-Sir4-mediated gene silencing and the loss of RNA interference.


2017 ◽  
Vol 46 (8) ◽  
pp. 3864-3877 ◽  
Author(s):  
Dongxue Wang ◽  
John R Horton ◽  
Yu Zheng ◽  
Robert M Blumenthal ◽  
Xing Zhang ◽  
...  

1988 ◽  
Vol 27 (5) ◽  
pp. 503-510 ◽  
Author(s):  
J. A. Hartley ◽  
J. W. Lown ◽  
W. B. Mattes ◽  
K. W. Kohn

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