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Title: Cloning, expression and characterization of the human transcription elongation factor, TFIIS
Authors: Yoon, Ho Sup
Baek, Kwanghee
Jeon, Choon Ju
Miyamoto, Kenichi
Ueno, Akemichi
Agarwal, Kan
Yoo, Ook Joon
Keywords: DRNTU::Science::Biological sciences::Biochemistry
Issue Date: 1991
Source: Yoo, O. J., Yoon, H. S., Baek, K., Jeon, C. J., Miyamoto, K., Ueno, A., & Agarwal, K. (1991). Cloning, expression and characterization of the human transcription elongation factor, TFIIS. Nucleic acids research, 19(5), 1073-1079.
Series/Report no.: Nucleic acids research
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.
DOI: 10.1093/nar/19.5.1073
Schools: School of Biological Sciences 
Rights: © 1991 Oxford University Press. This is the author created version of a work that has been peer reviewed and accepted for publication by Nucleic Acids Research, Oxford University Press. It incorporates referee’s comments but changes resulting from the publishing process, such as copyediting, structural formatting, may not be reflected in this document.  The published version is available at:
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:SBS Journal Articles

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