The histone folds in transcription factor TFIID

被引：31

作者：

Nakatani, Y

Bagby, S

Ikura, M

机构：

[1] UNIV TORONTO,ONTARIO CANC INST,DIV MOLEC & STRUCT BIOL,TORONTO,ON M5G 2M9,CANADA

[2] UNIV TORONTO,DEPT MED BIOPHYS,TORONTO,ON M5G 2M9,CANADA

[3] UNIV TSUKUBA,CTR TSUKUBA ADV RES ALLIANCE,TSUKUBA,IBARAKI 305,JAPAN

[4] UNIV TSUKUBA,INST APPL BIOCHEM,TSUKUBA,IBARAKI 305,JAPAN

来源：

JOURNAL OF BIOLOGICAL CHEMISTRY | 1996年 / 271卷 / 12期

关键词：

D O I：

10.1074/jbc.271.12.6575

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The transcription factor TFIID is a multimeric protein complex containing the TATA box-binding polypeptide (TBP) and TBP-associated factors. We have previously reported that the N-terminal regions of dTAF(II)62 and dTAF(II)42 have sequence similarities with histones H4 and H3. Here, we demonstrate that the histone-homologous regions of dTAF(II)62 and dTAF(II)42 form a heteromeric complex both in vitro and in a yeast two-hybrid system. Neither dTAF(II)62 nor dTAF(II)42 forms a homomeric complex, in agreement with a nucleosomal histone character. Moreover, circular dichroism measurements show that the heteromeric complex is dominated by cy-helical secondary structure. These results strongly suggest the existence of a histone-like surface on TFIID.

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页码：6575 / 6578

页数：4

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