Conserved structures of mediator and RNA polymerase II holoenzyme

Science

Volumn 283, Issue 5404, 1999, Pages 985-987

  Asturias, Francisco J ^a,b   Jiang, Yi Wei ^a   Myers, Lawrence C ^a   Gustafsson, Claes M ^a,c   Kornberg, Roger D ^a  

^a STANFORD UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b SCRIPPS RESEARCH INSTITUTE   (United States)

^c UNIVERSITY OF GOTHENBURG   (Sweden)

Author keywords

[No Author keywords available]

Indexed keywords

RNA POLYMERASE II;

ANIMAL CELL; ARTICLE; CARBOXY TERMINAL SEQUENCE; DNA BINDING; ELECTRON MICROSCOPY; ENZYME CONFORMATION; ENZYME STRUCTURE; EUKARYOTE; IMAGE PROCESSING; MOUSE; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN DOMAIN; REGULATORY MECHANISM; TRANSCRIPTION REGULATION;

ANIMALS; DNA-DIRECTED RNA POLYMERASES; FUNGAL PROTEINS; HOLOENZYMES; HYDROGEN-ION CONCENTRATION; MICE; MICROSCOPY, ELECTRON; PROTEIN CONFORMATION; PROTEIN FOLDING; TEMPERATURE; TRANS-ACTIVATORS; TRANSCRIPTION FACTORS;

EID: 0038832859     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.283.5404.985     Document Type: Article

References (17)

1. P. M. Flanagan, R. J. Kelleher III, M. H. Sayre, H. Tschochner, R. D. Kornberg, Nature 350, 436 (1991).
2. Y. J. Kim, S. Bjorklund, Y. Li, M. H. Sayre, R. D. Kornberg, Cell 77, 599 (1994).
3. C. M. Thompson, A. J. Koleske, D. M. Chao, R. A. Young, ibid. 73, 1361 (1993).
4. Y. Li et al., Proc. Natl. Acad. Sci. U.S.A. 92, 10864 (1995).
5. L. C. Myers et al., Genes Dev. 12, 45 (1998).
6. Y. W. Jiang et al., Proc. Natl. Acad. Sci. U.S.A. 95, 8538 (1998).
7. L. C. Myers, K. Leuther, D. A. Bushnell, C. M. Gustafsson, R. D. Kornberg, METHODS: A Companion to Methods in Enzymology 12, 212 (1997).
8. Purified Mediator was assayed in reactions reconstituted with essentially pure transcription proteins (7). Maximal transcriptional activation and maximal stimulation of basal transcription were obtained with levels of Mediator that were less than stoichiometric with core RNA polymerase II, which is indicative of a high percentage of active Mediator molecules.
9. About 85% of the particles were clearly recognizable as belonging to the reported average conformation and orientation. Most of the remaining particles appeared to be distorted but were easily recognized as variants of the average, most likely affected by the sample preparation procedure (adsorption to the grid and negative staining).
10. J. Frank et al., J. Struct. Biol. 116, 190 (1996).
11. The resolution of all average projection maps, calculated by Fourier ring correlation analysis of partial averages (10), was about 40 Å.
12. S. A. Darst, A. M. Edwards, E. W. Kubalek, R. D. Kornberg, Cell 66, 121 (1991).
13. C. D. Meredith et al., J. Mol. Biol. 258, 413 (1996).
14. F. J. Asturias, Y. W. Jiang, L. C. Myers, C. M. Gustafsson, R. D. Komberg, data not shown.
15. F. J. Asturias et al., unpublished data.
16. J. Q. Svejstrup et al., Proc. Natl. Acad. Sci. U.S.A. 94, 6075 (1997).
17. Supported by NIH grants Al21144 and GM36659 to R.D.K.