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Cloning, expression and characterization of the human transcription elongation factor, TFIIS

Authors :
Akemichi Ueno
Choon Ju Jeon
Kan Agarwal
Kenichi Miyamoto
Kwanghee Baek
Ook Joon Yoo
Ho Sup Yoon
School of Biological Sciences
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

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