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Science 8 June 2001:
Vol. 292. no. 5523, pp. 1844 - 1846
DOI: 10.1126/science.1062384

Perspectives

STRUCTURAL BIOLOGY:
A Marvellous Machine for Making Messages

Aaron Klug

The wonderful x-ray structures of RNA polymerase published in the past 3 years have revealed a wealth of information about how genes are transcribed. In an eloquent Perspective, Klug describes the latest tour de force from Kornberg's laboratory: the crystal structure of yeast RNA polymerase II in action.


The author is at the MRC Laboratory of Molecular Biology, Cambridge CB2 2QH, UK.

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THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Phosphorylation of the C-terminal Domain of RNA Polymerase II Plays Central Roles in the Integrated Events of Eucaryotic Gene Expression.
Y. Hirose and Y. Ohkuma (2007)
J. Biochem. 141, 601-608
   Abstract »    Full Text »    PDF »
The initiation-elongation transition: Lateral mobility of RNA in RNA polymerase II complexes is greatly reduced at +8/+9 and absent by +23.
M. Pal and D. S. Luse (2003)
PNAS 100, 5700-5705
   Abstract »    Full Text »    PDF »
A New Class of Transcription Initiation Factors, Intermediate between TATA Box-binding Proteins (TBPs) and TBP-like Factors (TLFs), Is Present in the Marine Unicellular Organism, the Dinoflagellate Crypthecodinium cohnii.
D. Guillebault, S. Sasorith, E. Derelle, J.-M. Wurtz, J.-C. Lozano, S. Bingham, L. Tora, and H. Moreau (2002)
J. Biol. Chem. 277, 40881-40886
   Abstract »    Full Text »    PDF »
Structural basis of transcription: alpha -Amanitin-RNA polymerase II cocrystal at 2.8 A resolution.
D. A. Bushnell, P. Cramer, and R. D. Kornberg (2002)
PNAS
   Abstract »    Full Text »    PDF »
Structural basis of transcription: alpha -Amanitin-RNA polymerase II cocrystal at 2.8 A resolution.
D. A. Bushnell, P. Cramer, and R. D. Kornberg (2002)
PNAS 99, 1218-1222
   Abstract »    Full Text »    PDF »



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