Identification and purification of a yeast protein that affects elongation by RNA polymerase II.
We have purified from whole cell extracts of Saccharomyces cerevisiae a protein which alters the elongation properties of yeast RNA polymerase II in vitro. The yeast elongation stimulatory activity, YES, correlates with a 116-kDa protein and acts on both yeast and Drosophila RNA polymerase II during transcription of double-stranded dC-tailed templates. The stimulatory activity is specific for RNA polymerase II since it has no significant effect on the elongation properties of yeast RNA polymerase I or yeast RNA polymerase III. Elongation by RNA polymerase II can be stimulated by RNase H on dC-tailed templates; however, the stimulatory activity of YES is not due to RNase H activity. YES does not stimulate RNA polymerase II in the presence of manganese ions and therefore is distinct from the smaller elongation factor, S-II or DmS-II. YES is most similar to Drosophila factor 5 (mammalian TFIIF, or RAP30/74), an initiation factor that is also able to increase the rate of elongation of RNA polymerase II.
Chafin
D R
DR
Department of Biochemistry, University of Iowa, Iowa City 52242.
Claussen
T J
TJ
Price
D H
DH
D000818:Animals; D004331:Drosophila melanogaster / Q000378:metabolism; D004722:Endoribonucleases / Q000378:metabolism; D004789:Enzyme Activation; D005656:Fungal Proteins / Q000302:isolation & purification* / Q000378:metabolism; D066298:In Vitro Techniques; D012319:RNA Polymerase II / Q000378:metabolism*; D016914:Ribonuclease H; D014157:Transcription Factors / Q000302:isolation & purification* / Q000378:metabolism; D014158:Transcription, Genetic
D005656:Fungal Proteins; D014157:Transcription Factors; D012319:RNA Polymerase II; D004722:Endoribonucleases; D016914:Ribonuclease H