Millisecond phase kinetic analysis of elongation catalyzed by human, yeast, and Escherichia coli RNA polymerase.
作者： Maria Kireeva , Yuri A. Nedialkov , Xue Qian Gong , Chunfen Zhang , Yalin Xiong
DOI: 10.1016/J.YMETH.2009.04.008
关键词: Biochemistry 、 Biology 、 Phosphodiester bond 、 RNA polymerase II 、 RNA polymerase 、 Elongation 、 Elongation factor 、 Polymerase 、 Biophysics 、 Yeast 、 Saccharomyces cerevisiae
摘要: Strategies for assembly and analysis of human, yeast, bacterial RNA polymerase elongation complexes are described, methods shown millisecond phase kinetic analyses using rapid chemical quench flow. Human, polymerases function very similarly in NTP-Mg2+ commitment phosphodiester bond formation. A "running start, two-bond, double-quench" protocol is described its advantages discussed. These studies provide information about stable loading, synthesis, the processive transition between bonds, sequence-specific effects on transcription dynamics.
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