Transcription processivity: protein-DNA interactions holding together the elongation complex - PubMed (original) (raw)
Transcription processivity: protein-DNA interactions holding together the elongation complex
E Nudler et al. Science. 1996.
Abstract
The elongation of RNA chains during transcription occurs in a ternary complex containing RNA polymerase (RNAP), DNA template, and nascent RNA. It is shown here that elongating RNAP from Escherichia coli can switch DNA templates by means of end-to-end transposition without loss of the transcript. After the switch, transcription continues on the new template. With the use of defined short DNA fragments as switching templates, RNAP-DNA interactions were dissected into two spatially distinct components, each contributing to the stability of the elongating complex. The front (F) interaction occurs ahead of the growing end of RNA. This interaction is non-ionic and requires 7 to 9 base pairs of intact DNA duplex. The rear (R) interaction is ionic and requires approximately six nucleotides of the template DNA strand behind the active site and one nucleotide ahead of it. The nontemplate strand is not involved. With the use of protein-DNA crosslinking, the F interaction was mapped to the conserved zinc finger motif in the NH2-terminus of the beta' subunit and the R interaction, to the COOH-terminal catalytic domain of the beta subunit. Mutational disruption of the zinc finger selectively destroyed the F interaction and produced a salt-sensitive ternary complex with diminished processivity. A model of the ternary complex is proposed here that suggests that trilateral contacts in the active center maintain the nonprocessive complex, whereas a front-end domain including the zinc finger ensures processivity.
Comment in
- The shrewd grasp of RNA polymerase.
Landick R, Roberts JW. Landick R, et al. Science. 1996 Jul 12;273(5272):202-3. doi: 10.1126/science.273.5272.202. Science. 1996. PMID: 8668996 Review. No abstract available.
Similar articles
- Characterization of halted T7 RNA polymerase elongation complexes reveals multiple factors that contribute to stability.
Mentesana PE, Chin-Bow ST, Sousa R, McAllister WT. Mentesana PE, et al. J Mol Biol. 2000 Oct 6;302(5):1049-62. doi: 10.1006/jmbi.2000.4114. J Mol Biol. 2000. PMID: 11183774 - The role of the largest RNA polymerase subunit lid element in preventing the formation of extended RNA-DNA hybrid.
Naryshkina T, Kuznedelov K, Severinov K. Naryshkina T, et al. J Mol Biol. 2006 Aug 25;361(4):634-43. doi: 10.1016/j.jmb.2006.05.034. Epub 2006 Jun 5. J Mol Biol. 2006. PMID: 16781733 - Model for the mechanism of bacteriophage T7 RNAP transcription initiation and termination.
Sousa R, Patra D, Lafer EM. Sousa R, et al. J Mol Biol. 1992 Mar 20;224(2):319-34. doi: 10.1016/0022-2836(92)90997-x. J Mol Biol. 1992. PMID: 1560455 - The shrewd grasp of RNA polymerase.
Landick R, Roberts JW. Landick R, et al. Science. 1996 Jul 12;273(5272):202-3. doi: 10.1126/science.273.5272.202. Science. 1996. PMID: 8668996 Review. No abstract available. - Hold on!: RNA polymerase interactions with the nascent RNA modulate transcription elongation and termination.
Grohmann D, Werner F. Grohmann D, et al. RNA Biol. 2010 May-Jun;7(3):310-5. doi: 10.4161/rna.7.3.11912. Epub 2010 May 26. RNA Biol. 2010. PMID: 20473037 Free PMC article. Review.
Cited by
- Probing the nucleobase selectivity of RNA polymerases with dual-coding substrates.
Mäkinen JJ, Rosenqvist P, Virta P, Metsä-Ketelä M, Belogurov GA. Mäkinen JJ, et al. J Biol Chem. 2024 Sep 12;300(10):107755. doi: 10.1016/j.jbc.2024.107755. Online ahead of print. J Biol Chem. 2024. PMID: 39260691 Free PMC article. - Factor-stimulated intrinsic termination: getting by with a little help from some friends.
Mandell ZF, Zemba D, Babitzke P. Mandell ZF, et al. Transcription. 2022 Aug-Oct;13(4-5):96-108. doi: 10.1080/21541264.2022.2127602. Epub 2022 Sep 25. Transcription. 2022. PMID: 36154805 Free PMC article. Review. - DSIF modulates RNA polymerase II occupancy according to template G + C content.
Deng N, Zhang Y, Ma Z, Lin R, Cheng TH, Tang H, Snyder MP, Cohen SN. Deng N, et al. NAR Genom Bioinform. 2022 Jul 27;4(3):lqac054. doi: 10.1093/nargab/lqac054. eCollection 2022 Sep. NAR Genom Bioinform. 2022. PMID: 35910045 Free PMC article. - Mutations compensating for the fitness cost of rifampicin resistance in Escherichia coli exert pleiotropic effect on RNA polymerase catalysis.
Kurepina N, Chudaev M, Kreiswirth BN, Nikiforov V, Mustaev A. Kurepina N, et al. Nucleic Acids Res. 2022 Jun 10;50(10):5739-5756. doi: 10.1093/nar/gkac406. Nucleic Acids Res. 2022. PMID: 35639764 Free PMC article. - β-CASP proteins removing RNA polymerase from DNA: when a torpedo is needed to shoot a sitting duck.
Wiedermannová J, Krásný L. Wiedermannová J, et al. Nucleic Acids Res. 2021 Oct 11;49(18):10221-10234. doi: 10.1093/nar/gkab803. Nucleic Acids Res. 2021. PMID: 34551438 Free PMC article. Review.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources