scholarly journals Crystal structures of the DNA-binding domain ofEscherichia coliproline utilization A flavoprotein and analysis of the role of Lys9 in DNA recognition

2006 ◽  
Vol 15 (11) ◽  
pp. 2630-2641 ◽  
Author(s):  
John D. Larson ◽  
Jermaine L. Jenkins ◽  
Jonathan P. Schuermann ◽  
Yuzhen Zhou ◽  
Donald F. Becker ◽  
...  
Keyword(s):  
Dna Binding ◽  
Crystal Structures ◽  
Dna Recognition ◽  
Binding Domain ◽  
Dna Binding Domain

Myb−DNA Recognition:  Role of Tryptophan Residues and Structural Changes of the Minimal DNA Binding Domain of c-Myb

Biochemistry ◽  
1999 ◽  
Vol 38 (6) ◽  
pp. 1921-1929 ◽  
Author(s):  
Loussinée Zargarian ◽  
Véronique Le Tilly ◽  
Nadège Jamin ◽  
Alain Chaffotte ◽  
Odd S. Gabrielsen ◽  
...  
Keyword(s):  
Dna Binding ◽  
Structural Changes ◽  
Dna Recognition ◽  
Binding Domain ◽  
Dna Binding Domain ◽  
Tryptophan Residues

scholarly journals Role of GCR2 in transcriptional activation of yeast glycolytic genes.

1992 ◽  
Vol 12 (9) ◽  
pp. 3834-3842 ◽  
Author(s):  
H Uemura ◽  
Y Jigami
Keyword(s):  
Dna Binding ◽  
Fusion Protein ◽  
Transcriptional Activation ◽  
Binding Domain ◽  
Dna Binding Domain ◽  
Gene Products ◽  
Lacz Expression ◽  
Genetic Method ◽  
Potential Interactions

The Saccharomyces cerevisiae GCR2 gene affects expression of most of the glycolytic genes. We report the nucleotide sequence of GCR2, which can potentially encode a 58,061-Da protein. There is a small cluster of asparagines near the center and a C-terminal region that would be highly charged but overall neutral. Fairly homologous regions were found between Gcr2 and Gcr1 proteins. To test potential interactions, the genetic method of S. Fields and O. Song (Nature [London] 340:245-246, 1989), which uses protein fusions of candidate gene products with, respectively, the N-terminal DNA-binding domain of Gal4 and the C-terminal activation domain II, assessing restoration of Gal4 function, was used. In a delta gal4 delta gal80 strain, double transformation by plasmids containing, respectively, a Gal4 (transcription-activating region)/Gcr1 fusion and a Gal4 (DNA-binding domain)/Gcr2 fusion activated lacZ expression from an integrated GAL1/lacZ fusion, indicating reconstitution of functional Gal4 through the interaction of Gcr1 and Gcr2 proteins. The Gal4 (transcription-activating region)/Gcr1 fusion protein alone complemented the defects of both gcr1 and gcr2 strains. Furthermore, a Rap1/Gcr2 fusion protein partially complemented the defects of gcr1 strains. These results suggest that Gcr2 has transcriptional activation activity and that the GCR1 and GCR2 gene products function together.

scholarly journals Functional Domains of c-myc Promoter Binding Protein 1 Involved in Transcriptional Repression and Cell Growth Regulation

1999 ◽  
Vol 19 (4) ◽  
pp. 2880-2886 ◽  
Author(s):  
Asish K. Ghosh ◽  
Robert Steele ◽  
Ratna B. Ray
Keyword(s):  
Amino Acids ◽  
Cell Growth ◽  
Dna Binding ◽  
Transcriptional Repression ◽  
Growth Regulation ◽  
Transcriptional Repressor ◽  
Binding Domain ◽  
Dna Binding Domain ◽  
Repressor Activity

ABSTRACT We initially identified c-myc promoter binding protein 1 (MBP-1), which negatively regulates c-myc promoter activity, from a human cervical carcinoma cell expression library. Subsequent studies on the biological role of MBP-1 demonstrated induction of cell death in fibroblasts and loss of anchorage-independent growth, reduced invasive ability, and tumorigenicity of human breast carcinoma cells. To investigate the potential role of MBP-1 as a transcriptional regulator, a chimeric protein containing MBP-1 fused to the DNA binding domain of the yeast transactivator factor GAL4 was constructed. This fusion protein exhibited repressor activity on the herpes simplex virus thymidine kinase promoter via upstream GAL4 DNA binding sites. Structure-function analysis of mutant MBP-1 in the context of the GAL4 DNA binding domain revealed that MBP-1 transcriptional repressor domains are located in the N terminus (amino acids 1 to 47) and C terminus (amino acids 232 to 338), whereas the activation domain lies in the middle (amino acids 140 to 244). The N-terminal domain exhibited stronger transcriptional repressor activity than the C-terminal region. When the N-terminal repressor domain was transferred to a potent activator, transcription was strongly inhibited. Both of the repressor domains contained hydrophobic regions and had an LXVXL motif in common. Site-directed mutagenesis in the repressor domains indicated that the leucine residues in the LXVXL motif are required for transcriptional repression. Mutation of the leucine residues in the common motif of MBP-1 also abrogated the repressor activity on the c-mycpromoter. In addition, the leucine mutant forms of MBP-1 failed to suppress cell growth in fibroblasts like wild-type MBP-1. Taken together, our results indicate that MBP-1 is a complex cellular factor containing multiple transcriptional regulatory domains that play an important role in cell growth regulation.

scholarly journals Rgg protein structure–function and inhibition by cyclic peptide compounds

2015 ◽  
Vol 112 (16) ◽  
pp. 5177-5182 ◽  
Author(s):  
Vijay Parashar ◽  
Chaitanya Aggarwal ◽  
Michael J. Federle ◽  
Matthew B. Neiditch
Keyword(s):  
Dna Binding ◽  
Structure Function ◽  
Cyclosporin A ◽  
Crystal Structures ◽  
Disulfide Bond ◽  
Binding Domain ◽  
Dna Binding Domain ◽  
X Ray ◽  
Peptide Pheromone ◽  
Dimerization Interface

Peptide pheromone cell–cell signaling (quorum sensing) regulates the expression of diverse developmental phenotypes (including virulence) in Firmicutes, which includes common human pathogens, e.g.,Streptococcus pyogenesandStreptococcus pneumoniae. Cytoplasmic transcription factors known as “Rgg proteins” are peptide pheromone receptors ubiquitous in Firmicutes. Here we present X-ray crystal structures of aStreptococcusRgg protein alone and in complex with a tight-binding signaling antagonist, the cyclic undecapeptide cyclosporin A. To our knowledge, these represent the first Rgg protein X-ray crystal structures. Based on the results of extensive structure–function analysis, we reveal the peptide pheromone-binding site and the mechanism by which cyclosporin A inhibits activation of the peptide pheromone receptor. Guided by the Rgg–cyclosporin A complex structure, we predicted that the nonimmunosuppressive cyclosporin A analog valspodar would inhibit Rgg activation. Indeed, we found that, like cyclosporin A, valspodar inhibits peptide pheromone activation of conserved Rgg proteins in medically relevantStreptococcusspecies. Finally, the crystal structures presented here revealed that the Rgg protein DNA-binding domains are covalently linked across their dimerization interface by a disulfide bond formed by a highly conserved cysteine. The DNA-binding domain dimerization interface observed in our structures is essentially identical to the interfaces previously described for other members of the XRE DNA-binding domain family, but the presence of an intermolecular disulfide bond buried in this interface appears to be unique. We hypothesize that this disulfide bond may, under the right conditions, affect Rgg monomer–dimer equilibrium, stabilize Rgg conformation, or serve as a redox-sensitive switch.

Structural Role of a Buried Salt Bridge in the 434 Repressor DNA-binding Domain

1996 ◽  
Vol 264 (5) ◽  
pp. 1002-1012 ◽  
Author(s):  
Konstantin Pervushin ◽  
Martin Billeter ◽  
Gregg Siegal ◽  
Kurt Wüthrich
Keyword(s):  
Dna Binding ◽  
Salt Bridge ◽  
Binding Domain ◽  
Dna Binding Domain ◽  
Structural Role ◽  
434 Repressor

The cavity in the hydrophobic core of Myb DNA-binding domain is reserved for DNA recognition and trans-activation

1996 ◽  
Vol 3 (2) ◽  
pp. 178-187 ◽  
Author(s):  
Kazuhiro Ogata ◽  
Chie Kanei-Ishii ◽  
Motoko Sasaki ◽  
Hideki Hatanaka ◽  
Aritaka Nagadoi ◽  
...  
Keyword(s):  
Dna Binding ◽  
Dna Recognition ◽  
Binding Domain ◽  
Dna Binding Domain ◽  
Hydrophobic Core
Sign in / Sign up

Export Citation Format

Share Document