scholarly journals The global repressor FliZ antagonizes gene expression by σ S -containing RNA polymerase due to overlapping DNA binding specificity

2012 ◽  
Vol 40 (11) ◽  
pp. 4783-4793 ◽  
Author(s):  
Christina Pesavento ◽  
Regine Hengge
Keyword(s):  
Gene Expression ◽  
Dna Binding ◽  
Rna Polymerase ◽  
Binding Specificity ◽  
Dna Binding Specificity

rUBF, an RNA polymerase I transcription factor from rats, produces DNase I footprints identical to those produced by xUBF, its homolog from frogs

1990 ◽  
Vol 10 (7) ◽  
pp. 3810-3812
Author(s):  
C S Pikaard ◽  
S D Smith ◽  
R H Reeder ◽  
L Rothblum
Keyword(s):  
Transcription Factor ◽  
Dna Binding ◽  
Rna Polymerase ◽  
Affinity Purification ◽  
Binding Specificity ◽  
Rna Polymerase I ◽  
Dna Binding Specificity ◽  
Apparent Homogeneity ◽  
And Function ◽  
Polymerase I

Rat cells contain a DNA-binding polymerase I transcription factor, rUBF, with properties similar to UBF homologs that have been purified from both human (hUBF) and frog (xUBF) cells. In this note we report the affinity purification of rUBF to apparent homogeneity and show that UBFs from both rat and frog have identical footprinting characteristics on templates from either species. Furthermore, xUBF was able to stimulate transcription from rat RNA polymerase I promoters in a partially fractionated rat extract that was UBF dependent. These results strengthen the conclusion that all vertebrate cells contain a UBF homolog whose DNA-binding specificity and function have been strongly conserved.

A factor with Sp1 DNA-binding specificity stimulates Xenopus U6 snRNA in vivo transcription by RNA polymerase III

1992 ◽  
Vol 228 (2) ◽  
pp. 387-394 ◽  
Author(s):  
Alain Lescure ◽  
Graham Tebb ◽  
Iain W. Mattaj ◽  
Alain Krol ◽  
Philippe Carbon
Keyword(s):  
Dna Binding ◽  
Rna Polymerase ◽  
Rna Polymerase Iii ◽  
Binding Specificity ◽  
U6 Snrna ◽  
Dna Binding Specificity ◽  
Polymerase Iii

The B-cell and neuronal forms of the octamer-binding protein Oct-2 differ in DNA-binding specificity and functional activity

1991 ◽  
Vol 11 (8) ◽  
pp. 3925-3930
Author(s):  
C L Dent ◽  
K A Lillycrop ◽  
J K Estridge ◽  
N S Thomas ◽  
D S Latchman
Keyword(s):  
Gene Expression ◽  
Dna Binding ◽  
B Cell ◽  
Functional Activity ◽  
Critical Role ◽  
Neuronal Cell ◽  
Binding Specificity ◽  
Cell Protein ◽  
Mobility Shift ◽  
Dna Binding Specificity

B lymphocytes contain an octamer-binding transcription factor, Oct-2, that is absent in most other cell types and plays a critical role in the B-cell-specific transcription of the immunoglobulin genes. A neuronal form of this protein has also been detected in brain and neuronal cell lines by using a DNA mobility shift assay, and an Oct-2 mRNA is observed in these cells by Northern (RNA) blotting and in situ hybridization. We show that the neuronal form of Oct-2 differs from that found in B cells with respect to both DNA-binding specificity and functional activity. In particular, whereas the B-cell protein activates octamer-containing promoters, the neuronal protein inhibits octamer-mediated gene expression. The possible role of the neuronal form of Oct-2 in the regulation of neuronal gene expression and its relationship to B-cell Oct-2 are discussed.

scholarly journals The B-cell and neuronal forms of the octamer-binding protein Oct-2 differ in DNA-binding specificity and functional activity.

1991 ◽  
Vol 11 (8) ◽  
pp. 3925-3930 ◽  
Author(s):  
C L Dent ◽  
K A Lillycrop ◽  
J K Estridge ◽  
N S Thomas ◽  
D S Latchman
Keyword(s):  
Gene Expression ◽  
Dna Binding ◽  
B Cell ◽  
Functional Activity ◽  
Critical Role ◽  
Neuronal Cell ◽  
Binding Specificity ◽  
Cell Protein ◽  
Mobility Shift ◽  
Dna Binding Specificity

B lymphocytes contain an octamer-binding transcription factor, Oct-2, that is absent in most other cell types and plays a critical role in the B-cell-specific transcription of the immunoglobulin genes. A neuronal form of this protein has also been detected in brain and neuronal cell lines by using a DNA mobility shift assay, and an Oct-2 mRNA is observed in these cells by Northern (RNA) blotting and in situ hybridization. We show that the neuronal form of Oct-2 differs from that found in B cells with respect to both DNA-binding specificity and functional activity. In particular, whereas the B-cell protein activates octamer-containing promoters, the neuronal protein inhibits octamer-mediated gene expression. The possible role of the neuronal form of Oct-2 in the regulation of neuronal gene expression and its relationship to B-cell Oct-2 are discussed.

scholarly journals rUBF, an RNA polymerase I transcription factor from rats, produces DNase I footprints identical to those produced by xUBF, its homolog from frogs.

1990 ◽  
Vol 10 (7) ◽  
pp. 3810-3812 ◽  
Author(s):  
C S Pikaard ◽  
S D Smith ◽  
R H Reeder ◽  
L Rothblum
Keyword(s):  
Transcription Factor ◽  
Dna Binding ◽  
Rna Polymerase ◽  
Affinity Purification ◽  
Binding Specificity ◽  
Rna Polymerase I ◽  
Dna Binding Specificity ◽  
Apparent Homogeneity ◽  
And Function ◽  
Polymerase I

Rat cells contain a DNA-binding polymerase I transcription factor, rUBF, with properties similar to UBF homologs that have been purified from both human (hUBF) and frog (xUBF) cells. In this note we report the affinity purification of rUBF to apparent homogeneity and show that UBFs from both rat and frog have identical footprinting characteristics on templates from either species. Furthermore, xUBF was able to stimulate transcription from rat RNA polymerase I promoters in a partially fractionated rat extract that was UBF dependent. These results strengthen the conclusion that all vertebrate cells contain a UBF homolog whose DNA-binding specificity and function have been strongly conserved.

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