| Autor: |
Darst SA; Beckman Laboratories for Structural Biology, Department of Cell Biology, Stanford University, California 94305., Edwards AM, Kubalek EW, Kornberg RD |
| Jazyk: |
angličtina |
| Zdroj: |
Cell [Cell] 1991 Jul 12; Vol. 66 (1), pp. 121-8. |
| DOI: |
10.1016/0092-8674(91)90144-n |
| Abstrakt: |
The structure of yeast RNA polymerase II has been determined by three-dimensional reconstruction from electron micrographs of two-dimensional crystals at approximately 16 A resolution. The most prominent feature of the structure is an arm of protein density surrounding a channel about 25 A in diameter, similar to that found previously for E. coli RNA polymerase. The 25 A-diameter channel bifurcates on one face of the protein, connecting with a 25 A-wide groove and with a channel about half as wide. The 25 A channel and groove, and the narrow channel, may bind double- and single-stranded nucleic acids, respectively. A finger of protein density projecting from the molecule adjacent to the arm-like feature may represent the C-terminal domain of the largest subunit. These results provide a structural basis for analyses of the transcription process and its regulation. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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