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  • Factors involved in specific transcription by mammalian RNA polymerase II: purification and characterization of general transcription factor TFIIE.

Factors involved in specific transcription by mammalian RNA polymerase II: purification and characterization of general transcription factor TFIIE.

Proceedings of the National Academy of Sciences of the United States of America (1990-12-01)
Y Ohkuma, H Sumimoto, M Horikoshi, R G Roeder
RESUMEN

Human transcription factor TFIIE, a ubiquitous factor required for transcription initiation by RNA polymerase II, was purified to homogeneity by a combination of conventional and HPLC steps. The purified TFIIE contained equimolar amounts of 57-kDa (TFIIE-alpha) and 34-kDa (TFIIE-beta) polypeptides that were judged to be functional subunits on the basis of their copurification with transcriptional activity and the recovery of activity following renaturation of polypeptides separated by reverse-phase HPLC. TFIIE-alpha had an independent TFIIE activity whereas TFIIE-beta had no activity alone but enhanced the activity of TFIIE-alpha. In conjunction with gel filtration studies, which indicated a molecular mass of approximately 180 kDa for the native protein, these results suggested that TFIIE is a heterotetramer containing two alpha and two beta polypeptides. Functional studies with the purified TFIIE demonstrated that it is a general initiation factor, required for all of the genes tested, but it failed to show any DNA-dependent ATPase activity.

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Sigma-Aldrich
TFIIE α, p56 human, recombinant, expressed in E. coli, ≥70% (SDS-PAGE)
Sigma-Aldrich
TFIIE β, p34 human, recombinant, expressed in E. coli, ≥70% (SDS-PAGE)
Sigma-Aldrich
TFIIE, α+β subunits human, recombinant, expressed in E. coli, ≥80% (SDS-PAGE)
Sigma-Aldrich
TFIIE, α (p56), α subunit, GST tagged human, recombinant, expressed in E. coli, ≥80% (SDS-PAGE)

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