A comparison of the loosely bound and tightly bound nonhistone proteins from Ehrlich ascites tumor chromatin.
The nonhistone proteins of Ehrlich ascites tumor chromatin have been separated into a loosely bound and two tightly bound protein fractions by sequential extraction of chromatin with 0.35 M NaCl and 2 M NaCl:5 M urea. The nonhistone proteins thus obtained were examined for their chemical composition and distribution of DNA polymerase, RNA polymerase, and protein kinase activities. In addition, the effect of these nonhistone proteins on transcription of DNA in vitro has been determined. The results indicate that these nonhistone proteins, fractionated on the basis of their extractability, exhibit varied compositional characteristics and play different functional roles in the synthesis of DNA and RNA and in the possible control of gene activity.
D000818:Animals; D002286:Carcinoma, Ehrlich Tumor / Q000378:metabolism*; D055598:Chemical Phenomena; D002621:Chemistry; D002843:Chromatin / Q000201:enzymology / Q000378:metabolism; D002868:Chromosomal Proteins, Non-Histone / Q000378:metabolism*; D004259:DNA-Directed DNA Polymerase / Q000378:metabolism; D012321:DNA-Directed RNA Polymerases / Q000378:metabolism; D008297:Male; D051379:Mice; D009363:Neoplasm Proteins / Q000378:metabolism*; D011494:Protein Kinases / Q000378:metabolism; D014158:Transcription, Genetic
D002843:Chromatin; D002868:Chromosomal Proteins, Non-Histone; D009363:Neoplasm Proteins; D011494:Protein Kinases; D012321:DNA-Directed RNA Polymerases; D004259:DNA-Directed DNA Polymerase