Expression and Characterization of a Fusion Protein Between the Catalytic Domain of Poly(ADP-Ribose) polymerase and the DNA Binding Domain of the Glucocorticoid Receptor

1994 ◽  
Vol 202 (2) ◽  
pp. 880-887 ◽  
Author(s):  
D. Rosenthal ◽  
T. Hong ◽  
B. Cherney ◽  
S.M. Zhang ◽  
T. Shima ◽  
...  
Keyword(s):  
Dna Binding ◽  
Glucocorticoid Receptor ◽  
Fusion Protein ◽  
Catalytic Domain ◽  
Binding Domain ◽  
Dna Binding Domain

scholarly journals Characterization of the Elk-1 ETS DNA-binding Domain

1995 ◽  
Vol 270 (11) ◽  
pp. 5805-5811 ◽  
Author(s):  
Paul Shore ◽  
Louise Bisset ◽  
Jeremy Lakey ◽  
Jonathan P. Waltho ◽  
Richard Virden ◽  
...  
Keyword(s):  
Dna Binding ◽  
Binding Domain ◽  
Dna Binding Domain

Characterization of Spi-B, a transcription factor related to the putative oncoprotein Spi-1/PU.1

1992 ◽  
Vol 12 (10) ◽  
pp. 4297-4304 ◽  
Author(s):  
D Ray ◽  
R Bosselut ◽  
J Ghysdael ◽  
M G Mattei ◽  
A Tavitian ◽  
...  
Keyword(s):  
Dna Binding ◽  
Cell Lines ◽  
Binding Domain ◽  
Dna Binding Domain ◽  
New Gene ◽  
Carboxy Terminal Region ◽  
Carboxy Terminal ◽  
Hematopoietic Cell Lines

We have cloned a human cDNA from a new gene, spi-B, on the basis of its homology with the DNA-binding domain of the Spi-1/PU.1 putative oncogene product. spi-B codes for a protein of 262 amino acids presenting 43% overall identity with Spi-1. Its highly basic carboxy-terminal region exhibits 34% sequence identity with the DNA-binding domain of the Ets-1 protein. We showed that the Spi-B protein is able to bind the purine-rich sequence (PU box) recognized by Spi-1/PU.1 and to activate transcription of a reporter plasmid containing PU boxes. Chromosome in situ hybridization allowed us to map spi-B to the 19q13.3-19q13.4 region of the human genome. spi-B, like spi-1, was found to be expressed in various murine and human hematopoietic cell lines except T lymphoid cell lines.

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 Structure refinement of the glucocorticoid receptor-DNA binding domain from NMR data by relaxation matrix calculations

1995 ◽  
Vol 247 (4) ◽  
pp. 689-700 ◽  
Author(s):  
Marc A.A. van Tilborg ◽  
Alexandre M.J.J. Bonvin ◽  
Karl Hård ◽  
Adrian L. Davis ◽  
Bonnie Maler ◽  
...  
Keyword(s):  
Dna Binding ◽  
Glucocorticoid Receptor ◽  
Structure Refinement ◽  
Binding Domain ◽  
Dna Binding Domain ◽  
Relaxation Matrix ◽  
Nmr Data

Structure and Dynamics of the Glucocorticoid Receptor DNA-Binding Domain:  Comparison of Wild Type and a Mutant with Altered Specificity†

Biochemistry ◽  
1997 ◽  
Vol 36 (37) ◽  
pp. 11188-11197 ◽  
Author(s):  
Helena Berglund ◽  
Magnus Wolf-Watz ◽  
Thomas Lundbäck ◽  
Susanne van den Berg ◽  
Torleif Härd
Keyword(s):  
Dna Binding ◽  
Glucocorticoid Receptor ◽  
Binding Domain ◽  
Dna Binding Domain ◽  
Wild Type ◽  
Structure And Dynamics
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