Structural organization of the RNA polymerase-promoter open complex.
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.
Naryshkin
N
N
Howard Hughes Medical Institute, Department of Chemistry, Rutgers University, Piscataway, New Jersey 08854, USA.
Revyakin
A
A
Kim
Y
Y
Mekler
V
V
Ebright
R H
RH
D000818:Animals; D001483:Base Sequence; D004247:DNA / Q000737:chemistry / Q000235:genetics*; D012321:DNA-Directed RNA Polymerases / Q000737:chemistry / Q000235:genetics*; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D011401:Promoter Regions, Genetic / Q000235:genetics*; D011487:Protein Conformation; D014158:Transcription, Genetic
D004247:DNA; D012321:DNA-Directed RNA Polymerases