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- Publisher Website: 10.1126/science.2194289
- Scopus: eid_2-s2.0-0025370531
- PMID: 2194289
- WOS: WOS:A1990DL48100037
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Article: Cloning of a transcriptionally active Human TATA binding factor
Title | Cloning of a transcriptionally active Human TATA binding factor |
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Authors | |
Issue Date | 1990 |
Citation | Science, 1990, v. 248, n. 4963, p. 1646-1650 How to Cite? |
Abstract | Transcrption factor IID (TFIID) binds to the TATA box promoter element and regulates the expression of most eukaryotic genes transcribed by RNA polymerase II. Complementary DNA (cDNA) encoding a human TFIID protein has been cloned. The human TFIID polypeptide has 339 amino acids and a molecular size of 37,745 daltons. The carboxyl-terminal 181 amino acids of the human TFIID protein shares 80% identity with the TFIID protein from Saccharomyces cerevisiae. The amino terminus contains an unusual repeat of 38 consecutive glutamine residues and an X-Thr-Pro repeat. Expression of DNA in reticulocyte lysates or in Escherichia coli yielded a protein that was competent for both DNA binding and transcription activation. |
Persistent Identifier | http://hdl.handle.net/10722/324972 |
ISSN | 2023 Impact Factor: 44.7 2023 SCImago Journal Rankings: 11.902 |
ISI Accession Number ID |
DC Field | Value | Language |
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dc.contributor.author | Kao, C. Cheng | - |
dc.contributor.author | Lieberman, Paul M. | - |
dc.contributor.author | Schmidt, Martin C. | - |
dc.contributor.author | Zhou, Qiang | - |
dc.contributor.author | Pei, Rui | - |
dc.contributor.author | Berk, Arnold J. | - |
dc.date.accessioned | 2023-02-27T07:28:40Z | - |
dc.date.available | 2023-02-27T07:28:40Z | - |
dc.date.issued | 1990 | - |
dc.identifier.citation | Science, 1990, v. 248, n. 4963, p. 1646-1650 | - |
dc.identifier.issn | 0036-8075 | - |
dc.identifier.uri | http://hdl.handle.net/10722/324972 | - |
dc.description.abstract | Transcrption factor IID (TFIID) binds to the TATA box promoter element and regulates the expression of most eukaryotic genes transcribed by RNA polymerase II. Complementary DNA (cDNA) encoding a human TFIID protein has been cloned. The human TFIID polypeptide has 339 amino acids and a molecular size of 37,745 daltons. The carboxyl-terminal 181 amino acids of the human TFIID protein shares 80% identity with the TFIID protein from Saccharomyces cerevisiae. The amino terminus contains an unusual repeat of 38 consecutive glutamine residues and an X-Thr-Pro repeat. Expression of DNA in reticulocyte lysates or in Escherichia coli yielded a protein that was competent for both DNA binding and transcription activation. | - |
dc.language | eng | - |
dc.relation.ispartof | Science | - |
dc.title | Cloning of a transcriptionally active Human TATA binding factor | - |
dc.type | Article | - |
dc.description.nature | link_to_subscribed_fulltext | - |
dc.identifier.doi | 10.1126/science.2194289 | - |
dc.identifier.pmid | 2194289 | - |
dc.identifier.scopus | eid_2-s2.0-0025370531 | - |
dc.identifier.volume | 248 | - |
dc.identifier.issue | 4963 | - |
dc.identifier.spage | 1646 | - |
dc.identifier.epage | 1650 | - |
dc.identifier.isi | WOS:A1990DL48100037 | - |