Structural basis of transcription: Backtracked RNA Polymerase II at 3.4 Angstrom Resolution

Science

Volumn 324, Issue 5931, 2009, Pages 1203-1206

  Wang, Dong ^a   Bushnell, David A ^a   Huang, Xuhui ^a   Westover, Kenneth D ^a   Levitt, Michael ^a   Kornberg, Roger D ^a  

^a STANFORD UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

RNA POLYMERASE II; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR SII; UNCLASSIFIED DRUG;

CRYSTAL STRUCTURE; DNA; ENZYME ACTIVITY; RNA; TRANSLOCATION; X-RAY SPECTROSCOPY;

ARTICLE; CRYSTAL STRUCTURE; DNA DAMAGE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CLEAVAGE; PROTEIN INTERACTION; PROTEIN LOCALIZATION; PROTEIN STRUCTURE; RNA SYNTHESIS;

5'-GUANYLIC ACID; BASE PAIR MISMATCH; CRYSTALLOGRAPHY, X-RAY; MODELS, MOLECULAR; NUCLEIC ACID CONFORMATION; OLIGORIBONUCLEOTIDES; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; RNA; RNA POLYMERASE II; SACCHAROMYCES CEREVISIAE; TRANSCRIPTION, GENETIC; TRANSCRIPTIONAL ELONGATION FACTORS;

EID: 66349138227     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.1168729     Document Type: Article

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54. This research was supported by NIH grants GM049985 and GM036559 to R.D.K. D.W. was supported by a special fellow award from the Leukemia and Lymphoma Society and the NIH Pathway to Independence Award (K99 GM085136). X.H. and M.L. were supported by NIH Roadmap for Medical Research Grant U54 GM072970 and NIH grant GM041455. Portions of the research were carried out at the Stanford Synchrotron Radiation Laboratory, a national user facility operated by Stanford University on behalf of the U.S. Department of Energy (DOE), Office of Basic Energy Sciences. The SSRL Structural Molecular Biology Program is supported by the DOE, Office of Biological and Environmental Research, and by the National Institutes of Health, National Center for Research Resources, Biomedical Technology Program, and the National Institute of General Medical Sciences. Portions of this research were conducted at the Advanced Light Source, a national user facility operated by Lawrence Berkeley National Laboratory, on behalf of the DOE, Office of Basic Energy Sciences. The Berkeley Center for Structural Biology is supported in part by the DOE, Office of Biological and Environmental Research, and by the National Institutes of Health, National Institute of General Medical Sciences. We thank C. D. Kaplan for providing TFIIS E291H mutant for structural studies. PDB accession codes: 13-nt oligomer backtracked pol II, 3GTJ; 18-nt oligomer backtracked pol II, 3GTK; 12-nt oligomer backtracked pol II, 3GTG; and 13-nt oligomer backtracked pol II with TFIIS, 3GTM.