How proteins recognize the TATA box

被引：280

作者：

Juo, ZS

Chiu, TK

Leiberman, PM

Baikalov, I

Berk, AJ

Dickerson, RE

机构：

[1] UNIV CALIF LOS ANGELES,DEPT CHEM,LOS ANGELES,CA 90095

[2] UNIV CALIF LOS ANGELES,INST MOL BIOL,LOS ANGELES,CA 90095

[3] UNIV CALIF LOS ANGELES,DEPT MICROBIOL & MOL GENET,LOS ANGELES,CA 90095

来源：

JOURNAL OF MOLECULAR BIOLOGY | 1996年 / 261卷 / 02期

关键词：

TATA box; TATA-binding proteins; DNA bending; DNA sequence recognition; A-tract bending;

D O I：

10.1006/jmbi.1996.0456

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 crystal structure of a complex of human TATA-binding protein with TATA-sequence DNA has been solved, complementing earlier TBP/DNA analyses from Saccharomyces cerevisiae and Arabidopsis thaliana. Special insight into TATA box specificity is provided by considering the TBP/DNA complex, not as a protein molecule with bound DNA, but as a DNA duplex with a particularly large minor groove ligand. This point of view provides explanations for: (1) why T-A base-pairs are required rather than C-G; (2) why an alternation of T and A bases is needed; (3) how TBP recognizes the upstream and downstream ends of the TATA box in order to bind properly; and (4) why the second half of the TATA box can be more variable than the first. (C) 1996 Academic Press Limited

引用

页码：239 / 254

页数：16

共 61 条

[1]

[Anonymous], DNA TOPOLOGY ITS BIO

[2] WEIGHT MATRIX DESCRIPTIONS OF 4 EUKARYOTIC RNA POLYMERASE-II PROMOTER ELEMENTS DERIVED FROM 502 UNRELATED PROMOTER SEQUENCES [J].