CONSERVED SEQUENCE MOTIFS IN THE SMALL SUBUNIT OF HUMAN GENERAL TRANSCRIPTION FACTOR TFIIE

被引：78

作者：

SUMIMOTO, H ^{[1
]}

OHKUMA, Y ^{[1
]}

SINN, E ^{[1
]}

KATO, H ^{[1
]}

SHIMASAKI, S ^{[1
]}

HORIKOSHI, M ^{[1
]}

ROEDER, RG ^{[1
]}

机构：

[1] WHITTIER INST DIABET & ENDOCRINOL,DEPT MOLEC ENDOCRINOL,LA JOLLA,CA 92037

来源：

NATURE | 1991年 / 354卷 / 6352期

关键词：

D O I：

10.1038/354401a0

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

A GENERAL initiation factor, TFIIE, is essential for transcription initiation by RNA polymerase II in conjunction with other general factors 1,2 . TFIIE is a heterotetramer containing two subunits of relative molecular mass 57,000 (TFIIE-alpha) and two of 34,000 (TFIIE-beta) 3,4. TFIIE-beta is required in conjunction with TFIIE-alpha for transcription initiation. Here we report the cloning and expression of a complementary DNA encoding a functional human TFIIE-beta. Recombinant TFIIE-beta could replace the natural TFIIE-beta for transcription in conjunction with TFIIE-alpha. Amino-acid sequence comparisons reveal regions with sequence similarities to: subregion 3 of bacterial or factors 6; a region of RAP30 (the small subunit of TFIIF) with sequence similarity to a sigma-factor subregion implicated in binding to RNA polymerase 7; and a portion of the basic region-helix-loop-helix motif found in several enhancer-binding proteins 8-10. These potential homologies have implications for the role of TFIIE in preinitiation complex assembly and function.

引用

页码：401 / 404

页数：4

共 30 条

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