4.8 Article

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

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SCIENCE
卷 327, 期 5962, 页码 206-209

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AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1182015

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资金

  1. NIH [GM049985, AI21144, K99 GM085136]
  2. Jane Coffin Childs Memorial Fund
  3. Department of Energy, Office of Biological and Environmental Research [DE-AC02-05CH11231, DE-AC02-06CH11357]
  4. NIH
  5. National Center for Research Resources, Biomedical Technology Program
  6. National Institute of General Medical Sciences

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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.

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