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

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-termin...

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Veröffentlicht in:Science (American Association for the Advancement of Science) 2010-01, Vol.327 (5962), p.206-209
Hauptverfasser: Liu, Xin, Bushnell, David A, Wang, Dong, Calero, Guillermo, Kornberg, Roger D
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Sprache:eng
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Zusammenfassung: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.
ISSN:0036-8075
0193-4511
1095-9203
DOI:10.1126/science.1182015