Iolation and charcterization of a DNA-binding non-histone protein from Tetrahymena pyriformis.
Three proteins (A, B and C) that bind specifically to single-stranded DNA have been isolated from the eukaryotic organism Tetrahymena pyriformis. Their molecular weights are 47 000, 41 000 and 32 000. The amino acid composition of the A protein indicates that it is a non-histone protein and sucrose gradient centrifugation shows that it binds to bacteriophage M13 DNA and to oligo (dT)100 in a cooperative manner. The exonucleolytic degradation of oligo (dT)100 is prevented when it is bound to the A protein. The effect of A protein on the exonucleolytic reaction confirms the cooperative manner of binding of A protein binding to oligo (dT)100 and shows that this process may be prevented by high ionic strength. The A protein seems to be without enzymatic activity.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001665:Binding Sites; D002846:Chromatography, Affinity; D003090:Coliphages; D004279:DNA, Viral; D005092:Exonucleases; D046911:Macromolecular Substances; D008970:Molecular Weight; D009838:Oligodeoxyribonucleotides; D011485:Protein Binding; D011506:Proteins / Q000032:analysis / Q000302:isolation & purification; D013769:Tetrahymena pyriformis / Q000032:analysis*; D013942:Thymine Nucleotides
D000596:Amino Acids; D004279:DNA, Viral; D046911:Macromolecular Substances; D009838:Oligodeoxyribonucleotides; D011506:Proteins; D013942:Thymine Nucleotides; D005092:Exonucleases