Cloning, expression and characterization of the human transcription elongation factor, TFIIS
| Autor: | Akemichi Ueno, Choon Ju Jeon, Kan Agarwal, Kenichi Miyamoto, Kwanghee Baek, Ook Joon Yoo, Ho Sup Yoon |
|---|---|
| Přispěvatelé: | School of Biological Sciences |
| Rok vydání: | 1991 |
| Předmět: |
Transcription
Genetic Molecular Sequence Data Gene Expression RNA polymerase II Molecular cloning Epitopes Mice Transcription (biology) Sequence Homology Nucleic Acid Complementary DNA Gene expression Escherichia coli Genetics Animals Humans Amino Acid Sequence Cloning Molecular Peptide sequence Transcription factor Cells Cultured Base Sequence biology DNA Science::Biological sciences::Biochemistry [DRNTU] Molecular biology Elongation factor biology.protein Cattle Electrophoresis Polyacrylamide Gel RNA Polymerase II Transcription Factors General Transcriptional Elongation Factors Transcription Factors |
| Zdroj: | Nucleic Acids Research. 19:1073-1079 |
| ISSN: | 1362-4962 0305-1048 |
| DOI: | 10.1093/nar/19.5.1073 |
| Popis: | The cDNA for the human elongation factor, TFIIS, has been cloned and expressed in E. coil with the T7 expression system. This 280-amino acid TFIIS protein is shorter by 21 residues than that of the mouse. The missing 21 residues are located in the amino-terminal region, which is not thought to be required for transcriptional stimulation. Apart from this gap, human and mouse proteins reveal 96% overall identity and 98.5% sequence similarity If conservative substitutions are taken into account. The bacterially expressed human protein and the purified calf thymus proteins are indistinguishable in their ability to stimulate transcript elongation by purified RNA polymerase II. Estimation of the native molecular size of the human protein in solution indicates that It exists as a dimer. Accepted version |
| Databáze: | OpenAIRE |
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