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
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
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页码:239 / 254
页数:16
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