scholarly journals Analysis of the DNA-binding sequence specificity of the archaeal transcriptional regulator Ss-LrpB from Sulfolobus solfataricus by systematic mutagenesis and high resolution contact probing

2006 ◽  
Vol 35 (2) ◽  
pp. 623-633 ◽  
Author(s):  
E. Peeters ◽  
C. Wartel ◽  
D. Maes ◽  
D. Charlier
Keyword(s):  
High Resolution ◽  
Dna Binding ◽  
Sulfolobus Solfataricus ◽  
Transcriptional Regulator ◽  
Sequence Specificity ◽  
Binding Sequence

scholarly journals DNA-binding sequence specificity of DUX4

2015 ◽  
Vol 6 (1) ◽  
Author(s):  
Yu Zhang ◽  
John K. Lee ◽  
Erik A. Toso ◽  
Joslynn S. Lee ◽  
Si Ho Choi ◽  
...  
Keyword(s):  
Dna Binding ◽  
Sequence Specificity ◽  
Binding Sequence

scholarly journals Functional divergence between the half-sites of the DNA-binding sequence for the yeast transcriptional regulator Rap1p

1999 ◽  
Vol 341 (3) ◽  
pp. 477-482 ◽  
Author(s):  
Fátima-Zahra IDRISSI ◽  
Benjamin PIÑA
Keyword(s):  
Dna Binding ◽  
Binding Sites ◽  
Functional Divergence ◽  
Consensus Sequence ◽  
Transcriptional Regulator ◽  
Dna Complexes ◽  
Dna Binding Sites ◽  
Binding Sequence ◽  
Half Site

The yeast transcriptional regulator Rap1p binds to the DNA consensus sequence ACACCCAYACAYYY. We have previously shown that DNA-binding sites in which all four Y (Y = T or C) positions were Ts (UASrpg sequences) synergized more efficiently to activate transcription than sequences in which all Ys were Cs (telomere sequences) [F.-Z. Idrissi, J. Fernández-Larrea and B. Piña (1998) J. Mol. Biol. 284, 925-935]. Here we provide evidence that the DNA consensus sequence for Rap1p behaves as a combination of two ACAYYY half-sites with different functionality, the presence of Ts in the second half-site being the determinant for the transcriptional behaviour of the UASrpg sequences. DNA structure in the different complexes with Rap1p varied from being relatively uniform to appear rather distorted, this also being dependent on the presence of Ts in the second half-site. These distortions did not cause sharp bends or kinks in the DNA molecule. Computer analysis suggests that high-affinity binding of Rap1p to UASrpg sequences requires a rearrangement of the C-terminal Myb domain of the protein. We propose that the structural alterations in Rap1p-DNA complexes, both in the DNA and in the protein, affect the transcription potential of the complex in an allosteric manner. We also propose that the dimeric nature of the Rap1 DNA-binding domain is a key structural feature that explains the disparate functions of its DNA-binding sites in vivo.

scholarly journals MarR-Like Transcriptional Regulator Involved in Detoxification of Aromatic Compounds in Sulfolobus solfataricus

2007 ◽  
Vol 189 (20) ◽  
pp. 7351-7360 ◽  
Author(s):  
Gabriella Fiorentino ◽  
Raffaele Ronca ◽  
Raffaele Cannio ◽  
Mosè Rossi ◽  
Simonetta Bartolucci
Keyword(s):  
Dna Binding ◽  
Aromatic Compounds ◽  
Sulfolobus Solfataricus ◽  
Transcriptional Regulator ◽  
Aromatic Aldehydes ◽  
Transcriptional Analysis ◽  
Regulatory Sequences ◽  
Gene Transcript ◽  
Cell Defense

ABSTRACT A DNA binding protein, BldR, was identified in the crenarchaeon Sulfolobus solfataricus as a protein 5- to 10-fold more abundant in cells grown in the presence of toxic aldehydes; it binds to regulatory sequences located upstream of an alcohol dehydrogenase gene (Sso2536). BldR is homologous to bacterial representatives of the MarR (multiple antibiotic resistance) family of transcriptional regulators that mediate response to multiple environmental stresses. Transcriptional analysis revealed that the bldR gene was transcribed in a bicistronic unit composed of the genes encoding the transcriptional regulator (Sso1352) and a putative multidrug transporter (Sso1351) upstream. By homology to bacterial counterparts, the bicistron was named the mar-like operon. The level of mar-like operon expression was found to be increased at least 10-fold in response to chemical stress by aromatic aldehydes. Under the same growth conditions, similar enhanced in vivo levels of Sso2536 gene transcript were also measured. The gene encoding BldR was expressed in E. coli, and the recombinant protein was purified to homogeneity. DNA binding assays demonstrated that the protein is indeed a transcription factor able to recognize site specifically both the Sso2536 and mar-like promoters at sites containing palindromic consensus sequences. Benzaldehyde, the substrate of ADHSs, stimulates DNA binding of BldR at both promoters. The role of BldR in the auto-activation as well as in the regulation of the Sso2536 gene, together with results of increased operon and gene expression under conditions of exposure to aromatic aldehydes, indicates a novel coordinate regulatory mechanism in cell defense against stress by aromatic compounds.

High-resolution detection of DNA binding sites of the global transcriptional regulator GlxR in Corynebacterium glutamicum

Microbiology ◽  
2013 ◽  
Vol 159 (Pt_1) ◽  
pp. 12-22 ◽  
Author(s):  
Britta Jungwirth ◽  
Claudia Sala ◽  
Thomas A. Kohl ◽  
Swapna Uplekar ◽  
Jan Baumbach ◽  
...  
Keyword(s):  
High Resolution ◽  
Dna Binding ◽  
Corynebacterium Glutamicum ◽  
Binding Sites ◽  
Transcriptional Regulator ◽  
Dna Binding Sites
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