scholarly journals Systematic mutational analysis of the LytTR DNA binding domain of Staphylococcus aureus virulence gene transcription factor AgrA

2014 ◽  
Vol 42 (20) ◽  
pp. 12523-12536 ◽  
Author(s):  
Sophie S. Nicod ◽  
Robert O. J. Weinzierl ◽  
Lynn Burchell ◽  
Andres Escalera-Maurer ◽  
Ellen H. James ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Transcription Factor ◽  
Dna Binding ◽  
Gene Transcription ◽  
Mutational Analysis ◽  
Virulence Gene ◽  
Binding Domain ◽  
Dna Binding Domain

scholarly journals The Yeast Heat Shock Transcription Factor Changes Conformation in Response to Superoxide and Temperature

2000 ◽  
Vol 11 (5) ◽  
pp. 1753-1764 ◽  
Author(s):  
Sengyong Lee ◽  
Tage Carlson ◽  
Noah Christian ◽  
Kristi Lea ◽  
Jennifer Kedzie ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Heat Shock ◽  
Dna Binding ◽  
Conformational Change ◽  
Mutational Analysis ◽  
Binding Domain ◽  
Heat Shock Transcription Factor ◽  
Dna Binding Domain ◽  
Yeast Saccharomyces Cerevisiae

In vitro DNA-binding assays demonstrate that the heat shock transcription factor (HSF) from the yeast Saccharomyces cerevisiae can adopt an altered conformation when stressed. This conformation, reflected in a change in electrophoretic mobility, requires that two HSF trimers be bound to DNA. Single trimers do not show this change, which appears to represent an alteration in the cooperative interactions between trimers. HSF isolated from stressed cells displays a higher propensity to adopt this altered conformation. Purified HSF can be stimulated in vitro to undergo the conformational change by elevating the temperature or by exposing HSF to superoxide anion. Mutational analysis maps a region critical for this conformational change to the flexible loop between the minimal DNA-binding domain and the flexible linker that joins the DNA-binding domain to the trimerization domain. The significance of these findings is discussed in the context of the induction of the heat shock response by ischemic stroke, hypoxia, and recovery from anoxia, all known to stimulate the production of superoxide.

NMR Structure of Transcription Factor Sp1 DNA Binding Domain†,‡

Biochemistry ◽  
2004 ◽  
Vol 43 (51) ◽  
pp. 16027-16035 ◽  
Author(s):  
Shinichiro Oka ◽  
Yasuhisa Shiraishi ◽  
Takuya Yoshida ◽  
Tadayasu Ohkubo ◽  
Yukio Sugiura ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Dna Binding ◽  
Binding Domain ◽  
Nmr Structure ◽  
Dna Binding Domain ◽  
Transcription Factor Sp1

scholarly journals Solution Structure of the DNA-Binding Domain of the Tomato Heat-Stress Transcription Factor HSF24

1996 ◽  
Vol 236 (3) ◽  
pp. 911-921 ◽  
Author(s):  
Jurgen Schultheiss ◽  
Olaf Kunert ◽  
Uwe Gase ◽  
Klaus-Dieter Scharf ◽  
Lutz Nover ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Heat Stress ◽  
Dna Binding ◽  
Solution Structure ◽  
Binding Domain ◽  
Dna Binding Domain

scholarly journals Adaptive evolution of transcription factor binding affinities

2017 ◽  
Author(s):  
Jungeui Hong ◽  
Nathan Brandt ◽  
Ally Yang ◽  
Tim Hughes ◽  
David Gresham
Keyword(s):  
Gene Expression ◽  
Transcription Factor ◽  
Dna Binding ◽  
Adaptive Evolution ◽  
Consensus Sequence ◽  
Binding Domain ◽  
Dna Binding Domain ◽  
Missense Mutations ◽  
Binding Affinities ◽  
Synonymous Mutations

Understanding the molecular basis of gene expression evolution is a central problem in evolutionary biology. However, connecting changes in gene expression to increased fitness, and identifying the functional basis of those changes, remains challenging. To study adaptive evolution of gene expression in real time, we performed long term experimental evolution (LTEE) of Saccharomyces cerevisiae (budding yeast) in ammonium-limited chemostats. Following several hundred generations of continuous selection we found significant divergence of nitrogen-responsive gene expression in lineages with increased fitness. In multiple independent lineages we found repeated selection for non-synonymous mutations in the zinc finger DNA binding domain of the activating transcription factor (TF), GAT1, that operates within incoherent feedforward loops to control expression of the nitrogen catabolite repression (NCR) regulon. Missense mutations in the DNA binding domain of GAT1 reduce its binding affinity for the GATAA consensus sequence in a promoter-specific manner, resulting in increased expression of ammonium permease genes via both direct and indirect effects, thereby conferring increased fitness. We find that altered transcriptional output of the NCR regulon results in antagonistic pleiotropy in alternate environments and that the DNA binding domain of GAT1 is subject to purifying selection in natural populations. Our study shows that adaptive evolution of gene expression can entail tuning expression output by quantitative changes in TF binding affinities while maintaining the overall topology of a gene regulatory network.

Structure, function, and dynamics of the dimerization and DNA-binding domain of oncogenic transcription factor v-Myc11Edited by P. E. Wright

2001 ◽  
Vol 307 (5) ◽  
pp. 1395-1410 ◽  
Author(s):  
Wolfgang Fieber ◽  
Martin L. Schneider ◽  
Theresia Matt ◽  
Bernhard Kräutler ◽  
Robert Konrat ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Dna Binding ◽  
Structure Function ◽  
Binding Domain ◽  
Factor V ◽  
Dna Binding Domain ◽  
Oncogenic Transcription Factor

scholarly journals Mutational analysis of the DNA binding domain A of chromosomal protein HMG1

1994 ◽  
Vol 22 (3) ◽  
pp. 285-292 ◽  
Author(s):  
Luca Falciola ◽  
Alastair I.H. Murchie ◽  
David M.J. Lilley ◽  
Marco E. Bianchi
Keyword(s):  
Dna Binding ◽  
Mutational Analysis ◽  
Binding Domain ◽  
Chromosomal Protein ◽  
Dna Binding Domain
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