Conformational changes inE.coliRNA polymerase during promoter recognition
- 1 January 1993
- journal article
- Published by Oxford University Press (OUP) in Nucleic Acids Research
- Vol. 21 (24) , 5748-5753
- https://doi.org/10.1093/nar/21.24.5748
Abstract
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.Keywords
This publication has 40 references indexed in Scilit:
- Development of RNA polymerase-promoter contacts during open complex formationJournal of Molecular Biology, 1991
- Unwinding of duplex DNA during transcription initiation at theEscherichia coligalactose operon overlapping promotersFEBS Letters, 1990
- Comparison of the open complexes formed by RNA polymerase at the Escherichia coli lac UV5 promoterJournal of Molecular Biology, 1987
- Temperature dependence of the rate constants of the Escherichia coli RNA polymerase-λP promoter interactionJournal of Molecular Biology, 1985
- Changes in the DNA structure of the lac UV5 promoter during formation of an open complex with Escherichia coli RNA polymeraseBiochemistry, 1985
- Topography of interaction of Escherichia coli RNA polymerase subunits with lac UV5 promoterFEBS Letters, 1981
- Histone-histone interactions within chromatin. Preliminary location of multiple contact sites between histones 2A, 2B and 4Biochemistry, 1979
- Studies on histone organization in the nucleosome using formaldehyde as a reversible cross-linking agentCell, 1978
- Subunits of RNA polymerase in function and structure: V. Maturation in vitro of core enzyme from Escherichia coliJournal of Molecular Biology, 1974
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970