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  Reversible stalling of transcription elongation complexes by high pressure

Erijman, L., & Clegg, R. M. (1998). Reversible stalling of transcription elongation complexes by high pressure. Biophysical Journal, 75, 453-462.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0012-FCAB-6 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-EC07-5
Genre: Journal Article

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Erijman, L.1, Author              
Clegg, R. M.2, Author
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1Department of Molecular Biology, MPI for biophysical chemistry, Max Planck Society, ou_578628              
2Max Planck Society, ou_persistent13              

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Free keywords: Coli RNA-polymerase; Ribonucleic-acid polymerase; Escherichia coli; Ternary complexes; Chain elongation; DNA replication; Termination; Protein; Temperature; Dependence; Biochemistry & biophysics
 Abstract: We have investigated the effect of high hydrostatic pressure on the stability of RNA polymerase molecules during transcription, RNA polymerase molecules participating in stalled or active ternary transcribing complexes do not dissociate from the template DNA and nascent RNA at pressures up to 180 MPa. A lower limit for the free energy of stabilization of an elongating ternary complex relative to the quaternary structure of the free RNAP molecules is estimated to be 20 kcal/mol. The rate of elongation decreases at high pressure; transcription completely halts at sufficiently high pressure. The overall rate of elongation has an apparent activation volume (Delta V double dagger) of 55-65 ml.mol(-1) (at 35 degrees C), The pressure-stalled transcripts are stable and resume elongation at the prepressure rate upon decompression. The efficiency of termination decreases at the rho-independent terminator tR2 after the transcription reaction has been exposed to high pressure. This suggests that high pressure modifies the ternary complex such that termination is affected in a manner different from that of elongation. The solvent and temperature dependence of the pressure-induced inhibition show evidence for major conformational changes in the core polymerase enzyme during RNA synthesis. It is proposed that the inhibition of the elongation phase of the transcription reaction at elevated pressures is related to a,reduction of the partial specific volume of the RNA polymerase molecule; under high pressure, the RNA polymerase molecule does not have the necessary structural flexibility required for the protein to translocate. [References: 45] 45

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Language(s): eng - English
 Dates: 2005-07-081998
 Publication Status: Published in print
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 Identifiers: eDoc: 224610
Other: 625
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Title: Biophysical Journal
Source Genre: Journal
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Pages: - Volume / Issue: 75 Sequence Number: - Start / End Page: 453 - 462 Identifier: -