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Nucleic Acids Research, 1993, Vol. 21, No. 24 5748-5753
© 1993

MOLECULAR BIOLOGY

Conformational changes in E.coli RNA polymerase during promoter recognition

Konstantin L. Brodolin*, Vasily M. Studitsky+ and Andrei D. Mirzabekov

W.A.Engelhardt Institute of Molecular Biology, Russian Academy of Sciences Moscow 117984, Russia

*Laboratoire de Biochimie Cellulaire, College de France, 11 Place Marcelin Berthelot, 75231 Paris cedex 05, France

Received August 3, 1993. Revised November 3, 1993. Accepted November 3, 1993.

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 ß' 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 RP0: there are strong {alpha}-ß' and ß-ß' interactions. In contrast, only ß-ß' cross-links were detected in the closed (RPc) and intermediate (RPl) complexes. In presence of lac repressor before or after formation of the RPo crosslinking pattern is similar with that of RPl (RPc) complex.

+Laboratory of Molecular Biology, NIDDK, National Institutes of Health, Bethesda, MD 20892, USA


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