Conformational changes in E. coli RNA polymerase during promoter recognition.
We analysed complexes formed during recognition of the lacUV5 promoter by E. coli RNA polymerase using formaldehyde as a DNA-protein and protein-protein cross-linking reagent. Most of the cross-linked complexes specific for the open complex (RPO) contain the beta' subunit of RNA polymerase cross-linked with promoter DNA in the regions: -50 to -49; -5 to -10; + 5 to +8 and +18 to +21. The protein-protein cross-linking pattern of contacting subunits is the same for the RNA polymerase in solution and in RPO: there are strong sigma-beta' and beta-beta' interactions. In contrast, only beta-beta' cross-links were detected in the closed (RPC) and intermediate (RPI) complexes. In presence of lac repressor before or after formation of the RPO cross-linking pattern is similar with that of RPI (RPC) complex.
Brodolin
K L
KL
W.A. Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow.
Studitsky
V M
VM
Mirzabekov
A D
AD
D012321:DNA-Directed RNA Polymerases / Q000737:chemistry* / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000201:enzymology*; D011401:Promoter Regions, Genetic; D011487:Protein Conformation; D012097:Repressor Proteins / Q000378:metabolism; D012996:Solutions; D013696:Temperature
D012097:Repressor Proteins; D012996:Solutions; D012321:DNA-Directed RNA Polymerases