ArticleNucleic acids research1992
Specific transcription from the adenovirus E2E promoter by RNA polymerase III requires a subpopulation of TFIID.
Article in Nucleic acids research, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 24 citations in OpenAlex.
- RNA polymerase III accurately initiates transcription from RNA polymerase II promoters in vitro.The Journal of biological chemistry · 2014Article
- Dr1 (NC2) is present at tRNA genes and represses their transcription in human cells.Nucleic acids research · 2010Article
- Gene therapy of benign gynecological diseases.Advanced drug delivery reviews · 2009Review
- A test of the model that RNA polymerase III transcription is regulated by selective induction of the 110 kDa subunit of TFIIIC.Nucleic acids research · 2006Article
- Unusual properties of adenovirus E2E transcription by RNA polymerase III.Journal of virology · 2003Article
- Interaction of the transcription factor TFIID with simian virus 40 (SV40) large T antigen interferes with replication of SV40 DNA in vitro.Journal of virology · 1999Article
- Flanking sequences of an Alu source stimulate transcription in vitro by interacting with sequence-specific transcription factors.Journal of molecular evolution · 1996Article
- Functional mRNA can be generated by RNA polymerase III.Molecular and cellular biology · 1995Article
- Mitotic regulation of a TATA-binding-protein-containing complex.Molecular and cellular biology · 1995Article
- In vivo transcription from the adenovirus E2 early promoter by RNA polymerase III.Proceedings of the National Academy of Sciences of the United States of America · 1994Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The early E2 (E2E) promoter of adenovirus type 2 possesses a TATA-like element and binding sites for the factors E2F and ATF. This promoter is transcribed by RNA polymerase II in high salt nuclear extracts, but by RNA polymerase III in standard nuclear extracts, as judged by sensitivity to low and high, respectively, concentrations of alpha-amanitin. Transcription by the two RNA polymerases initiated at the same site and depended, in both cases, on the TATA-like sequence and upstream elements. However, RNA polymerase III transcripts, unlike those synthesized by RNA polymerase II, terminated at two runs of Ts downstream of the initiation site. Although they are not essential, sequences downstream of the initiation site increased the efficiency of E2E transcription by RNA polymerase III. Such RNA polymerase III dependent transcription required a subpopulation of the general transcription factor, TFIID: TFIID that binds weakly to phosphocellulose (0.3 M eluate) complemented a TFIID-depleted extract to restore RNAp III transcription, whereas TFIID tightly associated with phosphocellulose (1 M eluate) was unable to do so.
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