Structural relationships of the three stimulatory factors of RNA polymerase II from Ehrlich ascites tumor cells.
The structural relationships of S-II, S-II', and S-I(b) stimulatory proteins of RNA polymerase II purified from Ehrlich ascites tumor cells were investigated. From analysis of the amino acid compositions and tryptic peptide maps of these proteins labeled with radioiodinated Bolton-Hunter reagent, it was concluded that S-I(b) is a part of S-II located at either the amino- or carboxyl-terminal and that only this region mainly contains radioiodinatable amino acid residues when labeled using 125I. On chymotryptic digestion, S-II was cleaved to 21- and 18-kDa fragments in the presence of DNA. The 21-kDa fragment was found to be sufficient for stimulation of RNA polymerase II. It was suggested that S-II' is formed by phosphorylation of S-II in the domain containing the 18-kDa fragment.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002286:Carcinoma, Ehrlich Tumor / Q000201:enzymology*; D002918:Chymotrypsin / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D007202:Indicators and Reagents; D051379:Mice; D010446:Peptide Fragments / Q000032:analysis; D011487:Protein Conformation; D012319:RNA Polymerase II / Q000378:metabolism*; D013388:Succinimides; D014357:Trypsin / Q000378:metabolism
D000596:Amino Acids; D007202:Indicators and Reagents; D010446:Peptide Fragments; D013388:Succinimides; C022581:Bolton-Hunter reagent; D012319:RNA Polymerase II; D002918:Chymotrypsin; D014357:Trypsin