Linked Life Data

1851172

Source:http://linkedlifedata.com/resource/pubmed/id/1851172

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
14
pubmed:dateCreated
1991-6-10
pubmed:abstractText
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.
pubmed:grant
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
266
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
9256-62
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Identification and purification of a yeast protein that affects elongation by RNA polymerase II.
pubmed:affiliation
Department of Biochemistry, University of Iowa, Iowa City 52242.
pubmed:publicationType
Journal Article, Comparative Study, In Vitro, Research Support, U.S. Gov't, P.H.S.