This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplemental material
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow E-mail this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Trinh, V.
Right arrow Articles by Coulombe, B.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Trinh, V.
Right arrow Articles by Coulombe, B.

 Previous Article  |  Next Article 

Microbiology and Molecular Biology Reviews, March 2006, p. 12-36, Vol. 70, No. 1
1092-2172/06/$08.00+0     doi:10.1128/MMBR.70.1.12-36.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Structural Perspective on Mutations Affecting the Function of Multisubunit RNA Polymerases{dagger}

Vincent Trinh,1 Marie-France Langelier,1 Jacques Archambault,2 and Benoit Coulombe1*

Gene Transcription Laboratory,1 Molecular Virology Laboratory, Institut de Recherches Cliniques de Montréal, Montréal, Québec, Canada H2W 1R72

High-resolution crystallographic structures of multisubunit RNA polymerases (RNAPs) have increased our understanding of transcriptional mechanisms. Based on a thorough review of the literature, we have compiled the mutations affecting the function of multisubunit RNA polymerases, many of which having been generated and studied prior to the publication of the first high-resolution structure, and highlighted the positions of the altered amino acids in the structures of both the prokaryotic and eukaryotic enzymes. The observations support many previous hypotheses on the transcriptional process, including the implication of the bridge helix and the trigger loop in the processivity of RNAP, the importance of contacts between the RNAP jaw-lobe module and the downstream DNA in the establishment of a transcription bubble and selection of the transcription start site, the destabilizing effects of ppGpp on the open promoter complex, and the link between RNAP processivity and termination. This study also revealed novel, remarkable features of the RNA polymerase catalytic mechanisms that will require additional investigation, including the putative roles of fork loop 2 in the establishment of a transcription bubble, the trigger loop in start site selection, and the uncharacterized funnel domain in RNAP processivity.

* Corresponding author. Mailing address: Gene Transcription Laboratory, Institut de Recherches Cliniques de Montréal, 110 Ave. des Pins Ouest, Montréal, Québec, Canada H2W 1R7. Phone: (514) 987-5662. Fax: (514) 987-5663. E-mail: benoit.coulombe{at}ircm.qc.ca.

{dagger} Supplemental material for this article may be found at http://mmbr.asm.org/.

Microbiology and Molecular Biology Reviews, March 2006, p. 12-36, Vol. 70, No. 1
1092-2172/06/$08.00+0     doi:10.1128/MMBR.70.1.12-36.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Hall, A. R., Griffiths, V. F., MacLean, R. C., Colegrave, N. (2010). Mutational neighbourhood and mutation supply rate constrain adaptation in Pseudomonas aeruginosa. Proc R Soc B 277: 643-650 [Abstract] [Full Text]  
  • Meyer, P. A., Ye, P., Suh, M.-H., Zhang, M., Fu, J. (2009). Structure of the 12-Subunit RNA Polymerase II Refined with the Aid of Anomalous Diffraction Data. J. Biol. Chem. 284: 12933-12939 [Abstract] [Full Text]  
  • Naji, S., Bertero, M. G., Spitalny, P., Cramer, P., Thomm, M. (2008). Structure-function analysis of the RNA polymerase cleft loops elucidates initial transcription, DNA unwinding and RNA displacement. Nucleic Acids Res 36: 676-687 [Abstract] [Full Text]  
  • Perkins, A. E., Nicholson, W. L. (2008). Uncovering New Metabolic Capabilities of Bacillus subtilis Using Phenotype Profiling of Rifampin-Resistant rpoB Mutants. J. Bacteriol. 190: 807-814 [Abstract] [Full Text]  
  • Nottebaum, S., Tan, L., Trzaska, D., Carney, H. C., Weinzierl, R. O. J. (2008). The RNA polymerase factory: a robotic in vitro assembly platform for high-throughput production of recombinant protein complexes. Nucleic Acids Res 36: 245-252 [Abstract] [Full Text]  
  • Xiong, Y., Burton, Z. F. (2007). A Tunable Ratchet Driving Human RNA Polymerase II Translocation Adjusted by Accurately Templated Nucleoside Triphosphates Loaded at Downstream Sites and by Elongation Factors. J. Biol. Chem. 282: 36582-36592 [Abstract] [Full Text]  
  • Kaneko, S., Chu, C., Shatkin, A. J., Manley, J. L. (2007). Human capping enzyme promotes formation of transcriptional R loops in vitro. Proc. Natl. Acad. Sci. USA 104: 17620-17625 [Abstract] [Full Text]  
  • Szalewska-Palasz, A., Johansson, L. U. M., Bernardo, L. M. D., Skarfstad, E., Stec, E., Brannstrom, K., Shingler, V. (2007). Properties of RNA Polymerase Bypass Mutants: IMPLICATIONS FOR THE ROLE OF ppGpp AND ITS CO-FACTOR DksA IN CONTROLLING TRANSCRIPTION DEPENDENT ON {sigma}54. J. Biol. Chem. 282: 18046-18056 [Abstract] [Full Text]  


Copyright © 2010 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»