Mutations in β"-Subunit of the Escherichia coli RNA-Polymerase Influence Interaction with the Downstream DNA Duplex in the Elongation Complex

Mutations in β"-Subunit of the Escherichia coli RNA-Polymerase Influence Interaction with the... RNA polymerase (RNAP) exhibits absolute processivity being capable of synthesizing RNA 103–105 nucleotides in length without breaking contact with the DNA template. Stability of the elongation complex is thought to depend, in particular, on the RNAP–DNA interactions downstream along the run of transcription. We studied the effects of several deletions and insertions in the RNAP β"-subunit N-terminal region, which presumably interacts with the downstream DNA duplex in the elongation complex. Most of the mutations obtained led to gross defects in RNAP assembly and disturbed catalytic activity of the enzyme. The mutations reduced stability of both promoter and elongation complexes, probably because they altered the contacts between RNAP and the downstream DNA duplex. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Russian Journal of Genetics Springer Journals

Mutations in β"-Subunit of the Escherichia coli RNA-Polymerase Influence Interaction with the Downstream DNA Duplex in the Elongation Complex

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Publisher
Kluwer Academic Publishers-Plenum Publishers
Copyright
Copyright © 2002 by MAIK “Nauka/Interperiodica”
Subject
Biomedicine; Human Genetics
ISSN
1022-7954
eISSN
1608-3369
D.O.I.
10.1023/A:1020665123810
Publisher site
See Article on Publisher Site

Abstract

RNA polymerase (RNAP) exhibits absolute processivity being capable of synthesizing RNA 103–105 nucleotides in length without breaking contact with the DNA template. Stability of the elongation complex is thought to depend, in particular, on the RNAP–DNA interactions downstream along the run of transcription. We studied the effects of several deletions and insertions in the RNAP β"-subunit N-terminal region, which presumably interacts with the downstream DNA duplex in the elongation complex. Most of the mutations obtained led to gross defects in RNAP assembly and disturbed catalytic activity of the enzyme. The mutations reduced stability of both promoter and elongation complexes, probably because they altered the contacts between RNAP and the downstream DNA duplex.

Journal

Russian Journal of GeneticsSpringer Journals

Published: Oct 13, 2004

References

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