期刊
SCIENCE
卷 327, 期 5962, 页码 206-209出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1182015
关键词
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资金
- NIH [GM049985, AI21144, K99 GM085136]
- Jane Coffin Childs Memorial Fund
- Department of Energy, Office of Biological and Environmental Research [DE-AC02-05CH11231, DE-AC02-06CH11357]
- NIH
- National Center for Research Resources, Biomedical Technology Program
- National Institute of General Medical Sciences
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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