Structure of an RNA Polymerase II-TFIIB Complex and the Transcription Initiation Mechanism

被引:162
作者
Liu, Xin [1 ]
Bushnell, David A. [1 ]
Wang, Dong [1 ]
Calero, Guillermo [1 ]
Kornberg, Roger D. [1 ]
机构
[1] Stanford Univ, Dept Biol Struct, Sch Med, Stanford, CA 94305 USA
关键词
CORE PROMOTER ELEMENT; PREINITIATION COMPLEX; ANGSTROM RESOLUTION; CRYSTAL-STRUCTURE; YEAST TFIIB; DNA; HOLOENZYME; ELONGATION; MODEL;
D O I
10.1126/science.1182015
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
Previous x-ray crystal structures have given insight into the mechanism of transcription and the role of general transcription factors in the initiation of the process. A structure of an RNA polymerase II-general transcription factor TFIIB complex at 4.5 angstrom resolution revealed the amino-terminal region of TFIIB, including a loop termed the "B finger," reaching into the active center of the polymerase where it may interact with both DNA and RNA, but this structure showed little of the carboxyl-terminal region. A new crystal structure of the same complex at 3.8 angstrom resolution obtained under different solution conditions is complementary with the previous one, revealing the carboxyl-terminal region of TFIIB, located above the polymerase active center cleft, but showing none of the B finger. In the new structure, the linker between the amino-and carboxyl-terminal regions can also be seen, snaking down from above the cleft toward the active center. The two structures, taken together with others previously obtained, dispel long-standing mysteries of the transcription initiation process.
引用
收藏
页码:206 / 209
页数:4
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