Architecture of RNA polymerase II and implications for the transcription mechanism

Science

Volumn 288, Issue 5466, 2000, Pages 640-649

  Cramer, Patrick ^a   Bushnell, David A ^a   Fu, Jianhua ^a   Gnatt, Averell L ^a   Maier Davis, Barbara ^a   Thompson, Nancy E ^b   Burgess, Richard R ^b   Edwards, Aled M ^c   David, Peter R ^a   Kornberg, Roger D ^a  

^a STANFORD UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b UNIVERSITY OF WISCONSIN MADISON   (United States)

^c UNIVERSITY OF TORONTO   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

RNA POLYMERASE;

ARTICLE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME SUBSTRATE COMPLEX; NONHUMAN; POLYMERIZATION; PRIORITY JOURNAL; RNA TRANSLATION; SACCHAROMYCES CEREVISIAE; TRANSCRIPTION REGULATION;

AMINO ACID MOTIFS; BINDING SITES; CATALYTIC DOMAIN; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; DNA, FUNGAL; ENZYME STABILITY; ESCHERICHIA COLI; HUMANS; MODELS, MOLECULAR; PROTEIN BINDING; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, SECONDARY; RNA POLYMERASE II; RNA, FUNGAL; RNA, MESSENGER; THERMUS; TRANSCRIPTION FACTORS; TRANSCRIPTION FACTORS, GENERAL; TRANSCRIPTION, GENETIC; TRANSCRIPTIONAL ELONGATION FACTORS;

EUKARYOTA; SACCHAROMYCES CEREVISIAE;

EID: 0034724953     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.288.5466.640     Document Type: Article

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96. For commercially unavailable heavy atom compounds, we thank P.J. Alaimo and R. Bergman (University of California, Berkeley); G. Huttner, P. Schöckers, and P. Hofmann (Universität Heidelberg); W. Scherer and W. A. Herrmann (Technische Universität München), G. Schneider (Stockholm University); R. Huber [Max Planck Institute (MPI) Martinsried]; B. Weberndörfer and H. Werner (Universität Würzburg); and W. Jahn (MPI Heidelberg). For assistance at Stanford Synchrotron Radiation Laboratory (SSRL), beamlines 1-5, 7-1, 9-1, and 9-2, we thank H. Bellamy, A. Cohen, P. Ellis, P. Kuhn, T. McPhillips, K. Hodgson, M. Soltis, and the other members of the SSRL user support staff. This research is based in part on work done at SSRL, which is funded by the U.S. Department of Energy Office of Basic Energy Sciences. The structural biology program is supported by the NIH National Center for Research Resources Biomedical Technology Program and the DOE Office of Biological and Environmental Research. For help at beamline 5.0.2 of the Advanced Light Source (ALS) at Berkeley, we thank T. Earnest. We thank C. Vonrhein for help with program SHARP. We thank R. Weinzierl and S. Onesti for sending us coordinates of the Rpb5 crystal structure before publication. We thank C. D. Mackereth and L. P. McIntosh for sending us coordinates of the Rpb10 NMR structure before publication. We thank M. Levitt, Y. Lorch, and B. Shaanan for comments on the manuscript. We gratefully acknowledge S. Darst for many contributions and for a copy of his manuscript on bacterial RNA polymerase-nucleic acid interaction before publication. P.C. was supported by a postdoctoral fellowship of the Deutsche Forschungsgemeinschaft (DFG). D.A.B. was supported by postdoctoral fellowship PF-00-014-01-GMC from the American Cancer Society. The contribution of A.L.G. was sponsored by U.S. AMRC Breast Cancer Initiative and does not necessarily reflect the policy of the government. This research was supported by NIH grant GM49985 to R.D.K. Coordinates of Cα atoms are available from http://kornberg.stanford. edu and have been deposited at the Protein Data Bank (accession code 1EN0).