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Cloning, expression and characterization of the human transcription elongation factor, TFIIS
- Source :
- Nucleic Acids Research. 19:1073-1079
- Publication Year :
- 1991
- Publisher :
- Oxford University Press (OUP), 1991.
-
Abstract
- 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
- Subjects :
- 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
Subjects
Details
- ISSN :
- 13624962 and 03051048
- Volume :
- 19
- Database :
- OpenAIRE
- Journal :
- Nucleic Acids Research
- Accession number :
- edsair.doi.dedup.....6aa5fb1ec9408216358130e1ed19702d
- Full Text :
- https://doi.org/10.1093/nar/19.5.1073