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Structural and functional characterization of the short acidic transcriptional activation region of yeast GCN4 protein
Derivatives of the yeast GCN4 transcription factor containing acidic regions of 35 to 40 amino acids fused directly to the DNA-binding domain are fully functional in vivo and may be important for interactions with the basic transcriptional machinery. Expand
Enhancement of bacterial gene expression by insertion elements or by mutation in a CAP-cAMP binding site.
- A. E. Reynolds, S. Mahadevan, S. LeGrice, A. Wright
- Biology, Medicine
- Journal of molecular biology
- 5 September 1986
The ethylmethane sulfonate-induced point mutations in bglR are alterations in a single base in the cAMP binding protein (CAP) binding site, leading to a stronger binding of the CAP-cAMP complex. Expand
Positive and negative regulation of the bgl operon in Escherichia coli
It is proposed that the bglS gene product has an additional role as a component of the beta-glucoside transport system. Expand
Characterisation of 3' end formation of the yeast HIS3 mRNA.
The 90-nt region appears to be sufficient to direct the formation of at least a subset of the HIS3 3' ends since mutants that carry deletions of flanking regions of this sequence show detectable levels of HIS3 mRNA. Expand
A bacterial gene involved in transcription antitermination: Regulation at a rho-independent terminator in the bgl operon of E. coli
The bglC gene product mediates positive regulation of the bgl operon by functioning as an antiterminator at the rho-independent terminator located within the leader. Expand
Characterization of the negative elements involved in silencing the bgl operon of Escherichia coli: possible roles for DNA gyrase, H‐NS, and CRP–cAMP in regulation
Evidence is provided which suggests that transcriptional activation by mutations at the cAMP receptor protein (CRP)‐binding site is mediated partly by antagonization of the negative effect of H‐NS by CRP–cAMP as a result of its increased affinity for the mutant site. Expand
The chbG Gene of the Chitobiose (chb) Operon of Escherichia coli Encodes a Chitooligosaccharide Deacetylase
The chb operon of Escherichia coli is involved in the utilization of the β-glucosides chitobiose and cellobiose, and it is shown that chbG encodes a monodeacetylase that is essential for growth on the acetylated chitooligosaccharides chittingobose and chitotriose but is dispensable for growth in the deacetylated form of chitosan dimer. Expand
Tc, an unusual promoter element required for constitutive transcription of the yeast HIS3 gene.
It is considered it possible that Tc may not interact with TFIID or some other typical sequence-specific transcription factor, but instead might influence transcription, either directly or indirectly, by its DNA structure. Expand
Mutations that alter the regulation of the chb operon of Escherichia coli allow utilization of cellobiose
- Aashiq H. Kachroo, A. Kancherla, N. S. Singh, U. Varshney, S. Mahadevan
- Biology, Medicine
- Molecular microbiology
- 1 December 2007
Biochemical characterization of one of the ChbR mutants, chbRN238S, showed that the mutant regulator makes stronger contact with the target DNA sequence within the chb promoter and has enhanced recognition of cellobiose 6‐phosphate as an inducer compared with the wild‐type regulator. Expand
Oxidative cleavage of DNA by a dipyridoquinoxaline copper(II) complex in the presence of ascorbic acid.
- B. Santra, Pattubala A. N. Reddy, G. Neelakanta, S. Mahadevan, M. Nethaji, A. R. Chakravarty
- Chemistry, Medicine
- Journal of inorganic biochemistry
- 28 April 2002
Complex [Cu(dpq)(2)(H(2)O)](ClO(4))(2).H(2)O (1), where dpq is dipyrido-[3,2-D:2',3'-f]-quinoxaline, has been prepared by reacting copper(II) perchlorate hexahydrate with dpq in methanol and… Expand