Conformational Plasticity and DNA-Binding Specificity of the Eukaryotic Transcription Factor Pax5

Biochemistry ◽  
2021 ◽  
Author(s):  
Cecilia Perez-Borrajero ◽  
Florian Heinkel ◽  
Jörg Gsponer ◽  
Lawrence P. McIntosh
Keyword(s):  
Transcription Factor ◽  
Dna Binding ◽  
Binding Specificity ◽  
Eukaryotic Transcription ◽  
Dna Binding Specificity ◽  
Conformational Plasticity

DNA binding specificity of cardiac transcription factor complex GATA4 and NKX2‐5

2020 ◽  
Vol 34 (S1) ◽  
pp. 1-1
Author(s):  
Jessica Marie Rodriguez Rios ◽  
Emili Patricia Rosado Rodríguez ◽  
José Arcadio Rodríguez Martínez
Keyword(s):  
Transcription Factor ◽  
Dna Binding ◽  
Binding Specificity ◽  
Dna Binding Specificity ◽  
Transcription Factor Complex

scholarly journals Determinants of DNA-binding specificity of ETS-domain transcription factors.

1996 ◽  
Vol 16 (7) ◽  
pp. 3338-3349 ◽  
Author(s):  
P Shore ◽  
A J Whitmarsh ◽  
R Bhaskaran ◽  
R J Davis ◽  
J P Waltho ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Dna Binding ◽  
Serum Response Factor ◽  
Binding Specificity ◽  
Mitogen Activated Protein Kinase ◽  
Critical Determinant ◽  
Binding Interface ◽  
Dna Binding Specificity ◽  
Mitogen Activated Protein ◽  
Ets Domain

Several mechanisms are employed by members of transcription factor families to achieve sequence-specific DNA recognition. In this study, we have investigated how members of the ETS-domain transcription factor family achieve such specificity. We have used the ternary complex factor (TCF) subfamily as an example. ERK2 mitogen-activated protein kinase stimulates serum response factor-dependent and autonomous DNA binding by the TCFs Elk-1 and SAP-la. Phosphorylated Elk-1 and SAP-la exhibit specificities of DNA binding similar to those of their isolated ETS domains. The ETS domains of Elk-1 and SAP-la and SAP-2 exhibit related but distinct DNA-binding specificities. A single residue, D-69 (Elk-1) or V-68 (SAP-1), has been identified as the critical determinant for the differential binding specificities of Elk-1 and SAP-1a, and an additional residue, D-38 (Elk-1) or Q-37 (SAP-1), further modulates their DNA binding. Creation of mutations D38Q and D69V is sufficient to confer SAP-la DNA-binding specificity upon Elk-1 and thereby allow it to bind to a greater spectrum of sites. Molecular modelling indicates that these two residues (D-38 and D-69) are located away from the DNA-binding interface of Elk-1. Our data suggest a mechanism in which these residues modulate DNA binding by influencing the interaction of other residues with DNA.

scholarly journals Decoding the Inversion Symmetry Underlying Transcription Factor DNA-Binding Specificity and Functionality in the Genome

iScience ◽  
2019 ◽  
Vol 15 ◽  
pp. 552-591 ◽  
Author(s):  
Laurel A. Coons ◽  
Adam B. Burkholder ◽  
Sylvia C. Hewitt ◽  
Donald P. McDonnell ◽  
Kenneth S. Korach
Keyword(s):  
Transcription Factor ◽  
Dna Binding ◽  
Binding Specificity ◽  
Inversion Symmetry ◽  
Dna Binding Specificity

rUBF, an RNA polymerase I transcription factor from rats, produces DNase I footprints identical to those produced by xUBF, its homolog from frogs

1990 ◽  
Vol 10 (7) ◽  
pp. 3810-3812
Author(s):  
C S Pikaard ◽  
S D Smith ◽  
R H Reeder ◽  
L Rothblum
Keyword(s):  
Transcription Factor ◽  
Dna Binding ◽  
Rna Polymerase ◽  
Affinity Purification ◽  
Binding Specificity ◽  
Rna Polymerase I ◽  
Dna Binding Specificity ◽  
Apparent Homogeneity ◽  
And Function ◽  
Polymerase I

Rat cells contain a DNA-binding polymerase I transcription factor, rUBF, with properties similar to UBF homologs that have been purified from both human (hUBF) and frog (xUBF) cells. In this note we report the affinity purification of rUBF to apparent homogeneity and show that UBFs from both rat and frog have identical footprinting characteristics on templates from either species. Furthermore, xUBF was able to stimulate transcription from rat RNA polymerase I promoters in a partially fractionated rat extract that was UBF dependent. These results strengthen the conclusion that all vertebrate cells contain a UBF homolog whose DNA-binding specificity and function have been strongly conserved.

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