Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
1994-3-22
pubmed:abstractText
The TATA-binding protein (TBP) plays a central role in transcription initiation by nuclear RNA polymerases I, II, and III. With knowledge of the three-dimensional structure of TBP, mutational analyses were focused on the highly exposed basic repeat domain in yeast TBP in order to identify amino acid residues which could discriminate transcription functions of different RNA polymerases. One mutation (K156L) was found to specifically abolish transcription by RNA polymerase I and another mutation (K138L) specifically abolished transcription by RNA polymerase III, while each maintained the ability to support in vitro transcription by the other two RNA polymerases. Along with previous studies, these results indicate that the basic repeat domain of TBP is important not only for transcription by RNA polymerase II but also for transcription by RNA polymerases I and III and, further, that the region has distinct sites for interactions which are specific for RNA polymerases I and III.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
18
pubmed:volume
269
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4891-4
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Involvement of the basic repeat domain of TATA-binding protein (TBP) in transcription by RNA polymerases I, II, and III.
pubmed:affiliation
Laboratory of Biochemistry and Molecular Biology, Rockefeller University, New York, New York 10021.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't