Abstract
A GENERAL initiation factor, TFIIE, is essential for transcription initiation by RNA polymerase II in conjunction with other general factors1,2. TFIIE is a heterotetramer containing two subunits of relative molecular mass 57,000 (TFIIE-α) and two of 34,000 (TFIIE-β)3,4. TFIIE-β is required in conjunction with TFIIE-α for transcription initiation. Here we report the cloning and expression of a complementary DNA encoding a functional human TFIIE-β. Recombinant TFIIE-β could replace the natural TFIIE-β for transcription in conjunction with TFIIE-α. Amino-acid sequence comparisons reveal regions with sequence similarities to: subregion 3 of bacterial factors6; a region of RAP30 (the small subunit of TFIIF) with sequence similarity to a a factor subregion implicated in binding to RNA polymerase7; and a portion of the basic region-helix-loop-helix motif found in several enhancer-binding proteins8,10. These potential homologies have implications for the role of TFIIE in preinitiation complex assembly and function.
| Original language | English |
|---|---|
| Pages (from-to) | 401-404 |
| Number of pages | 4 |
| Journal | Nature |
| Volume | 354 |
| Issue number | 6352 |
| DOIs | |
| Publication status | Published - Jan 1 1991 |
| Externally published | Yes |
Fingerprint
All Science Journal Classification (ASJC) codes
- General
Cite this
Conserved sequence motifs in the small subunit of human general transcription factor TFIIE. / Sumimoto, Hideki; Ohkuma, Yoshiaki; Sinn, Eric; Kato, Hiroyuki; Shimasaki, Shunichi; Horikoshi, Masami; Roeder, Robert G.
In: Nature, Vol. 354, No. 6352, 01.01.1991, p. 401-404.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Conserved sequence motifs in the small subunit of human general transcription factor TFIIE
AU - Sumimoto, Hideki
AU - Ohkuma, Yoshiaki
AU - Sinn, Eric
AU - Kato, Hiroyuki
AU - Shimasaki, Shunichi
AU - Horikoshi, Masami
AU - Roeder, Robert G.
PY - 1991/1/1
Y1 - 1991/1/1
N2 - A GENERAL initiation factor, TFIIE, is essential for transcription initiation by RNA polymerase II in conjunction with other general factors1,2. TFIIE is a heterotetramer containing two subunits of relative molecular mass 57,000 (TFIIE-α) and two of 34,000 (TFIIE-β)3,4. TFIIE-β is required in conjunction with TFIIE-α for transcription initiation. Here we report the cloning and expression of a complementary DNA encoding a functional human TFIIE-β. Recombinant TFIIE-β could replace the natural TFIIE-β for transcription in conjunction with TFIIE-α. Amino-acid sequence comparisons reveal regions with sequence similarities to: subregion 3 of bacterial factors6; a region of RAP30 (the small subunit of TFIIF) with sequence similarity to a a factor subregion implicated in binding to RNA polymerase7; and a portion of the basic region-helix-loop-helix motif found in several enhancer-binding proteins8,10. These potential homologies have implications for the role of TFIIE in preinitiation complex assembly and function.
AB - A GENERAL initiation factor, TFIIE, is essential for transcription initiation by RNA polymerase II in conjunction with other general factors1,2. TFIIE is a heterotetramer containing two subunits of relative molecular mass 57,000 (TFIIE-α) and two of 34,000 (TFIIE-β)3,4. TFIIE-β is required in conjunction with TFIIE-α for transcription initiation. Here we report the cloning and expression of a complementary DNA encoding a functional human TFIIE-β. Recombinant TFIIE-β could replace the natural TFIIE-β for transcription in conjunction with TFIIE-α. Amino-acid sequence comparisons reveal regions with sequence similarities to: subregion 3 of bacterial factors6; a region of RAP30 (the small subunit of TFIIF) with sequence similarity to a a factor subregion implicated in binding to RNA polymerase7; and a portion of the basic region-helix-loop-helix motif found in several enhancer-binding proteins8,10. These potential homologies have implications for the role of TFIIE in preinitiation complex assembly and function.
UR - http://www.scopus.com/inward/record.url?scp=0026046960&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0026046960&partnerID=8YFLogxK
U2 - 10.1038/354401a0
DO - 10.1038/354401a0
M3 - Article
C2 - 1956404
AN - SCOPUS:0026046960
VL - 354
SP - 401
EP - 404
JO - Nature
JF - Nature
SN - 0028-0836
IS - 6352
ER -