Abstract
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.
Publication types
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Animals
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Base Sequence
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Cattle
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Cells, Cultured
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Cloning, Molecular
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DNA / isolation & purification
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Electrophoresis, Polyacrylamide Gel
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Epitopes / immunology
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Escherichia coli / genetics*
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Gene Expression
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Humans
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Mice
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Molecular Sequence Data
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RNA Polymerase II / biosynthesis
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Sequence Homology, Nucleic Acid
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Transcription Factors / genetics*
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Transcription Factors / immunology
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Transcription Factors / metabolism
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Transcription Factors, General*
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Transcription, Genetic
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Transcriptional Elongation Factors*
Substances
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Epitopes
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Transcription Factors
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Transcription Factors, General
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Transcriptional Elongation Factors
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transcription factor S-II
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DNA
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RNA Polymerase II
Associated data
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GENBANK/S62405
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GENBANK/S62419
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GENBANK/S62424
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GENBANK/X56310
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GENBANK/X56998
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GENBANK/X56999
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GENBANK/X57198
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GENBANK/X57453
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GENBANK/X57454
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GENBANK/X57455