A constitutive damage-specific DNA-binding protein is synthesized at higher levels in UV-irradiated primate cells

1990 ◽  
Vol 10 (5) ◽  
pp. 2041-2048
Author(s):  
S Hirschfeld ◽  
A S Levine ◽  
K Ozato ◽  
M Protić
Keyword(s):  
Dna Binding ◽  
Protein Complex ◽  
Uv Light ◽  
Specific Binding ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Pyrimidine Dimer ◽  
Band Shift ◽  
Competition Analysis ◽  
Cellular Dna

Using a DNA band shift assay, we have identified a DNA-binding protein complex in primate cells which is present constitutively and has a high affinity for UV-irradiated, double-stranded DNA. Cells pretreated with UV light, mitomycin C, or aphidicolin have higher levels of this damage-specific DNA-binding protein complex, suggesting that the signal for induction can either be damage to the DNA or interference with cellular DNA replication. Physiochemical modifications of the DNA and competition analysis with defined substrates suggest that the most probable target site for the damage-specific DNA-binding protein complex is a 6-4'-(pyrimidine-2'-one)-pyrimidine dimer: specific binding could not be detected with probes which contain -TT- cyclobutane dimers, and damage-specific DNA binding did not decrease after photoreactivation of UV-irradiated DNA. This damage-specific DNA-binding protein complex is the first such inducible protein complex identified in primate cells. Cells from patients with the sun-sensitive cancer-prone disease, xeroderma pigmentosum (group E), are lacking both the constitutive and the induced damage-specific DNA-binding activities. These findings suggest a possible role for this DNA-binding protein complex in lesion recognition and DNA repair of UV-light-induced photoproducts.

scholarly journals A constitutive damage-specific DNA-binding protein is synthesized at higher levels in UV-irradiated primate cells.

1990 ◽  
Vol 10 (5) ◽  
pp. 2041-2048 ◽  
Author(s):  
S Hirschfeld ◽  
A S Levine ◽  
K Ozato ◽  
M Protić
Keyword(s):  
Dna Binding ◽  
Protein Complex ◽  
Uv Light ◽  
Specific Binding ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Pyrimidine Dimer ◽  
Band Shift ◽  
Competition Analysis ◽  
Cellular Dna

Using a DNA band shift assay, we have identified a DNA-binding protein complex in primate cells which is present constitutively and has a high affinity for UV-irradiated, double-stranded DNA. Cells pretreated with UV light, mitomycin C, or aphidicolin have higher levels of this damage-specific DNA-binding protein complex, suggesting that the signal for induction can either be damage to the DNA or interference with cellular DNA replication. Physiochemical modifications of the DNA and competition analysis with defined substrates suggest that the most probable target site for the damage-specific DNA-binding protein complex is a 6-4'-(pyrimidine-2'-one)-pyrimidine dimer: specific binding could not be detected with probes which contain -TT- cyclobutane dimers, and damage-specific DNA binding did not decrease after photoreactivation of UV-irradiated DNA. This damage-specific DNA-binding protein complex is the first such inducible protein complex identified in primate cells. Cells from patients with the sun-sensitive cancer-prone disease, xeroderma pigmentosum (group E), are lacking both the constitutive and the induced damage-specific DNA-binding activities. These findings suggest a possible role for this DNA-binding protein complex in lesion recognition and DNA repair of UV-light-induced photoproducts.

Single-Stranded DNA-Binding Protein Complex from Helicobacter pylori Suggests an ssDNA-Binding Surface

2009 ◽  
Vol 388 (3) ◽  
pp. 508-519 ◽  
Author(s):  
Kun-Wei Chan ◽  
Yi-Juan Lee ◽  
Chia-Hung Wang ◽  
Haimei Huang ◽  
Yuh-Ju Sun
Keyword(s):  
Helicobacter Pylori ◽  
Dna Binding ◽  
Protein Complex ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Single Stranded Dna ◽  
Ssdna Binding ◽  
Binding Surface

scholarly journals Interaction between anti-DNA and anti-DNA-binding protein autoantibodies in cryoglobulins from sera of patients with systemic lupus erythematosus.

1986 ◽  
Vol 164 (4) ◽  
pp. 1029-1042 ◽  
Author(s):  
W H Reeves ◽  
N Chiorazzi
Keyword(s):  
Systemic Lupus Erythematosus ◽  
Dna Binding ◽  
Lupus Erythematosus ◽  
Immune Complexes ◽  
Protein Complex ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Systemic Lupus ◽  
Variable Regions ◽  
Dna Antibodies

We have previously shown that sera from some patients with SLE and related disorders contain autoantibodies to a DNA-binding protein complex designated p70/p80. The present study shows that anti-p70/p80 autoantibodies are frequently accompanied by anti-DNA antibodies and cryoglobulins. When the cryoglobulins were isolated, they were found to be specifically enriched in both anti-p70/p80 and anti-DNA activities. The anti-p70/p80 and anti-DNA antibodies were found to be distinct populations of autoantibodies rather than a single crossreactive species, since they could be separated from one another by chromatography on DNA-cellulose. Certain human anti-DNA mAbs could inhibit the binding of autoimmune polyclonal anti-p70/p80 antibodies to p70/p80, suggesting that anti-DNA antibodies might also associate with the variable regions of some anti-p70/p80 antibodies in the cryoglobulins. Binding of one murine anti-p70/p80 mAb (111-12) also was inhibited by certain human anti-DNA mAbs, but the binding of another murine mAb (162-11) to a different epitope of p70/p80 was not. These studies suggest that certain anti-DNA antibodies may interact with the variable regions of a population of anti-p70/p80 antibodies. The cryoglobulins found in the sera containing both anti-p70/p80 and anti-DNA antibodies may represent immune complexes consisting, in part, of idiotype and antiidiotype.

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