CLONING, EXPRESSION AND CHARACTERIZATION OF THE HUMAN TRANSCRIPTION ELONGATION-FACTOR, TFIIS

The cDNA for the human elongation factor, TFIIS, has been cloned and expressed in E. coli 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.
Publisher
OXFORD UNIV PRESS UNITED KINGDOM
Issue Date
1991-03
Language
ENG
Keywords

RNA POLYMERASE-II; CALF THYMUS; FACTOR-SII; PURIFICATION; GENE

Citation

NUCLEIC ACIDS RESEARCH, v.19, no.5, pp.1073 - 1079

ISSN
0305-1048
DOI
10.1093/nar/19.5.1073
URI
http://hdl.handle.net/10203/5814
Appears in Collection
NE-Journal Papers(저널논문)
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