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Identification and purification of a yeast protein that affects elongation by RNA polymerase II
Journal article   Open access   Peer reviewed

Identification and purification of a yeast protein that affects elongation by RNA polymerase II

David R Chafin, Traci J Claussen and David H Price
The Journal of biological chemistry, Vol.266(14), pp.9256-9262
1991
DOI: 10.1016/S0021-9258(18)31578-3
PMID: 1851172
url
https://doi.org/10.1016/S0021-9258(18)31578-3View
Published (Version of record) Open Access

Abstract

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.
 Molecular Genetics Fundamental and applied biological sciences. Psychology Biological and medical sciences Transcription. Transcription factor. Splicing. Rna processing Molecular and cellular biology

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