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Updated: Jun 18, 2026

High-throughput Purification of Affinity-tagged Recombinant Proteins
Published on: August 26, 2012
Structural organization of the RNA polymerase-promoter open complex
N Naryshkin1, A Revyakin, Y Kim
1Howard Hughes Medical Institute, Department of Chemistry, Rutgers University, Piscataway, New Jersey 08854, USA.
Abstract:
We have used systematic site-specific protein-DNA photocrosslinking to define interactions between bacterial RNA polymerase (RNAP) and promoter DNA in the catalytically competent RNAP-promoter open complex (RPo). We have mapped more than 100 distinct crosslinks between individual segments of RNAP subunits and individual phosphates of promoter DNA. The results provide a comprehensive description of protein-DNA interactions in RPo, permit construction of a detailed model for the structure of RPo, and permit analysis of effects of a transcriptional activator on the structure of RPo.
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