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Journal Article

The dynamic machinery of mRNA elongation.

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Cramer,  P.
Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society;

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Citation

Armache, K. J., Kettenberger, H., & Cramer, P. (2005). The dynamic machinery of mRNA elongation. Current Opinion in Structural Biology, 15(2), 197-203. doi:10.1016/j.sbi.2005.03.002.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0015-848C-D
Abstract
Two complementary X-ray studies of the interaction between RNA polymerase II and nucleic acids have improved our understanding of mRNA elongation. These studies suggest how RNA polymerase II unwinds DNA, how it separates the RNA product from the DNA template and how it incorporates nucleoside triphosphate (NTP) substrates into the growing RNA chain. The tunable polymerase active center apparently allows repositioning of a catalytic metal ion, rotation of NTPs before their incorporation, RNA repositioning by a transcript cleavage factor, and modulation of enzyme activity by a bacterial small molecule regulator and its protein cofactor.