This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
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 Archambault, J
Right arrow Articles by Friesen, J D
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Archambault, J
Right arrow Articles by Friesen, J D

 Previous Article  |  Next Article 

Microbiol Mol Biol Rev. 1993 September; 57(3): 703-724

Genetics of eukaryotic RNA polymerases I, II, and III.

J Archambault and J D Friesen

Department of Genetics, Hospital for Sick Children, Toronto, Ontario, Canada.

SUMMARY

The transcription of nucleus-encoded genes in eukaryotes is performed by three distinct RNA polymerases termed I, II, and III, each of which is a complex enzyme composed of more than 10 subunits. The isolation of genes encoding subunits of eukaryotic RNA polymerases from a wide spectrum of organisms has confirmed previous biochemical and immunological data indicating that all three enzymes are closely related in structures that have been conserved in evolution. Each RNA polymerase is an enzyme complex composed of two large subunits that are homologous to the two largest subunits of prokaryotic RNA polymerases and are associated with smaller polypeptides, some of which are common to two or to all three eukaryotic enzymes. This remarkable conservation of structure most probably underlies a conservation of function and emphasizes the likelihood that information gained from the study of RNA polymerases from one organism will be applicable to others. The recent isolation of many mutations affecting the structure and/or function of eukaryotic and prokaryotic RNA polymerases now makes it feasible to begin integrating genetic and biochemical information from various species in order to develop a picture of these enzymes. The picture of eukaryotic RNA polymerases depicted in this article emphasizes the role(s) of different polypeptide regions in interaction with other subunits, cofactors, substrates, inhibitors, or accessory transcription factors, as well as the requirement for these interactions in transcription initiation, elongation, pausing, termination, and/or enzyme assembly. Most mutations described here have been isolated in eukaryotic organisms that have well-developed experimental genetic systems as well as amenable biochemistry, such as Saccharomyces cerevisiae, Drosophila melanogaster, and Caenorhabditis elegans. When relevant, mutations affecting regions of Escherichia coli RNA polymerase that are conserved among eukaryotes and prokaryotes are also presented. In addition to providing information about the structure and function of eukaryotic RNA polymerases, the study of mutations and of the pleiotropic phenotypes they imposed has underscored the central role played by these enzymes in many fundamental processes such as development and cellular differentiation.

Microbiol Mol Biol Rev. 1993 September; 57(3): 703-724




This article has been cited by other articles:

  • Arnett, D. R., Jennings, J. L., Tabb, D. L., Link, A. J., Weil, P. A. (2008). A Proteomics Analysis of Yeast Mot1p Protein-Protein Associations: Insights into Mechanism. Mol. Cell. Proteomics 7: 2090-2106 [Abstract] [Full Text]  
  • Kawauchi, J., Mischo, H., Braglia, P., Rondon, A., Proudfoot, N. J. (2008). Budding yeast RNA polymerases I and II employ parallel mechanisms of transcriptional termination. Genes Dev. 22: 1082-1092 [Abstract] [Full Text]  
  • Heras, S. R., Lopez, M. C., Olivares, M., Thomas, M. C. (2007). The L1Tc non-LTR retrotransposon of Trypanosoma cruzi contains an internal RNA-pol II-dependent promoter that strongly activates gene transcription and generates unspliced transcripts. Nucleic Acids Res 35: 2199-2214 [Abstract] [Full Text]  
  • Bobula, J., Tomala, K., Jez, E., Wloch, D. M., Borts, R. H., Korona, R. (2006). Why Molecular Chaperones Buffer Mutational Damage: A Case Study With a Yeast Hsp40/70 System. Genetics 174: 937-944 [Abstract] [Full Text]  
  • Kang, X., Hu, Y., Li, Y., Guo, X., Jiang, X., Lai, L., Xia, B., Jin, C. (2006). Structural, Biochemical, and Dynamic Characterizations of the hRPB8 Subunit of Human RNA Polymerases. J. Biol. Chem. 281: 18216-18226 [Abstract] [Full Text]  
  • Scholtens, D., Vidal, M., Gentleman, R. (2005). Local modeling of global interactome networks. Bioinformatics 21: 3548-3557 [Abstract] [Full Text]  
  • Makarova, K. S., Wolf, Y. I., Mekhedov, S. L., Mirkin, B. G., Koonin, E. V. (2005). Ancestral paralogs and pseudoparalogs and their role in the emergence of the eukaryotic cell. Nucleic Acids Res 33: 4626-4638 [Abstract] [Full Text]  
  • Bartlett, M. S., Thomm, M., Geiduschek, E. P. (2004). Topography of the Euryarchaeal Transcription Initiation Complex. J. Biol. Chem. 279: 5894-5903 [Abstract] [Full Text]  
  • Wu, L., Pan, J., Thoroddsen, V., Wysong, D. R., Blackman, R. K., Bulawa, C. E., Gould, A. E., Ocain, T. D., Dick, L. R., Errada, P., Dorr, P. K., Parkinson, T., Wood, T., Kornitzer, D., Weissman, Z., Willis, I. M., McGovern, K. (2003). Novel Small-Molecule Inhibitors of RNA Polymerase III. Eukaryot Cell 2: 256-264 [Abstract] [Full Text]  
  • Murakami, K. S., Masuda, S., Darst, S. A. (2002). Structural Basis of Transcription Initiation: RNA Polymerase Holoenzyme at 4 A Resolution. Science 296: 1280-1284 [Abstract] [Full Text]  
  • Darst, S. A., Opalka, N., Chacon, P., Polyakov, A., Richter, C., Zhang, G., Wriggers, W. (2002). Conformational flexibility of bacterial RNA polymerase. Proc. Natl. Acad. Sci. USA 99: 4296-4301 [Abstract] [Full Text]  
  • Minakhin, L., Bhagat, S., Brunning, A., Campbell, E. A., Darst, S. A., Ebright, R. H., Severinov, K. (2001). Bacterial RNA polymerase subunit omega and eukaryotic RNA polymerase subunit RPB6 are sequence, structural, and functional homologs and promote RNA polymerase assembly. Proc. Natl. Acad. Sci. USA 98: 892-897 [Abstract] [Full Text]  
  • Ingham, C. J., Furneaux, P. A. (2000). Mutations in the {beta} subunit of the Bacillus subtilis RNA polymerase that confer both rifampicin resistance and hypersensitivity to NusG. Microbiology 146: 3041-3049 [Abstract] [Full Text]  
  • Pappas, D. L. Jr., Hampsey, M. (2000). Functional Interaction between Ssu72 and the Rpb2 Subunit of RNA Polymerase II in Saccharomyces cerevisiae. Mol. Cell. Biol. 20: 8343-8351 [Abstract] [Full Text]  
  • Korzheva, N., Mustaev, A., Kozlov, M., Malhotra, A., Nikiforov, V., Goldfarb, A., Darst, S. A. (2000). A Structural Model of Transcription Elongation. Science 289: 619-625 [Abstract] [Full Text]  
  • Donaldson, I. M., Friesen, J. D. (2000). Zinc Stoichiometry of Yeast RNA Polymerase II and Characterization of Mutations in the Zinc-binding Domain of the Largest Subunit. J. Biol. Chem. 275: 13780-13788 [Abstract] [Full Text]  
  • Sugaya, K, Vigneron, M, Cook, P. (2000). Mammalian cell lines expressing functional RNA polymerase II tagged with the green fluorescent protein. J. Cell Sci. 113: 2679-2683 [Abstract]  
  • Gallegos, M.-T., Cannon, W. V., Buck, M. (1999). Functions of the sigma 54 Region I in Trans and Implications for Transcription Activation. J. Biol. Chem. 274: 25285-25290 [Abstract] [Full Text]  
  • Hirt, R. P., Logsdon, J. M. Jr., Healy, B., Dorey, M. W., Doolittle, W. F., Embley, T. M. (1999). Microsporidia are related to Fungi: Evidence from the largest subunit of RNA polymerase II and other proteins. Proc. Natl. Acad. Sci. USA 96: 580-585 [Abstract] [Full Text]  
  • Chervitz, S. A., Aravind, L., Sherlock, G., Ball, C. A., Koonin, E. V., Dwight, S. S., Harris, M. A., Dolinski, K., Mohr, S., Smith, T., Weng, S., Cherry, J. M., Botstein, D. (1998). Comparison of the Complete Protein Sets of Worm and Yeast: Orthology and Divergence. Science 282: 2022-2028 [Abstract] [Full Text]  
  • Dorjsuren, D., Lin, Y., Wei, W., Yamashita, T., Nomura, T., Hayashi, N., Murakami, S. (1998). RMP, a Novel RNA Polymerase II Subunit 5-Interacting Protein, Counteracts Transactivation by Hepatitis B Virus X Protein. Mol. Cell. Biol. 18: 7546-7555 [Abstract] [Full Text]  
  • Zhang, G., Darst, S. A. (1998). Structure of the Escherichia coli RNA Polymerase alpha  Subunit Amino-Terminal Domain. Science 281: 262-266 [Abstract] [Full Text]  
  • Mooney, R. A., Artsimovitch, I., Landick, R. (1998). Information Processing by RNA Polymerase: Recognition of Regulatory Signals during RNA Chain Elongation. J. Bacteriol. 180: 3265-3275 [Full Text]  
  • Hampsey, M. (1998). Molecular Genetics of the RNA Polymerase II General Transcriptional Machinery. Microbiol. Mol. Biol. Rev. 62: 465-503 [Abstract] [Full Text]  
  • Archambault, J., Jansma, D. B., Kawasoe, J. H., Arndt, K. T., Greenblatt, J., Friesen, J. D. (1998). Stimulation of Transcription by Mutations Affecting Conserved Regions of RNA Polymerase II. J. Bacteriol. 180: 2590-2598 [Abstract] [Full Text]  
  • Lang, W. H., Platt, T., Reeder, R. H. (1998). Escherichia coli rho factor induces release of yeast RNA polymerase II but not polymerase I or III. Proc. Natl. Acad. Sci. USA 95: 4900-4905 [Abstract] [Full Text]  
  • Sukhodolets, M. V., Jin, D. J. (1998). RapA, a Novel RNA Polymerase-Associated Protein, Is a Bacterial Homolog of SWI2/SNF2. J. Biol. Chem. 273: 7018-7023 [Abstract] [Full Text]  
  • Hartzog, G. A., Wada, T., Handa, H., Winston, F. (1998). Evidence that Spt4, Spt5, and Spt6 control transcription elongation by RNA polymerase II in Saccharomyces cerevisiae. Genes Dev. 12: 357-369 [Abstract] [Full Text]  
  • EBRIGHT, R.H. (1998). RNA Polymerase-DNA Interaction: Structures of Intermediate, Open, and Elongation Complexes. Cold Spring Harb Symp Quant Biol 63: 11-20 [Abstract]  
  • DARST, S.A., POLYAKOV, A., RICHTER, C., ZHANG, G. (1998). Structural Studies of Escherichia coli RNA Polymerase. Cold Spring Harb Symp Quant Biol 63: 269-276 [Abstract]  
  • Pan, G., Aso, T., Greenblatt, J. (1997). Interaction of Elongation Factors TFIIS and Elongin A with a Human RNA Polymerase II Holoenzyme Capable of Promoter-specific Initiation and Responsive to Transcriptional Activators. J. Biol. Chem. 272: 24563-24571 [Abstract] [Full Text]  
  • Wang, D., Severinov, K., Landick, R. (1997). Preferential interaction of the his pause RNA hairpin with RNA polymerase beta  subunit residues 904-950 correlates with strong transcriptional pausing. Proc. Natl. Acad. Sci. USA 94: 8433-8438 [Abstract] [Full Text]  
  • Acker, J., de Graaff, M., Cheynel, I., Khazak, V., Kedinger, C., Vigneron, M. (1997). Interactions between the Human RNA Polymerase II Subunits. J. Biol. Chem. 272: 16815-16821 [Abstract] [Full Text]  
  • Yang, X., Price, C. W. (1995). Streptolydigin Resistance Can Be Conferred by Alterations to Either the beta or beta` Subunits of Bacillus subtilis RNA Polymerase. J. Biol. Chem. 270: 23930-23933 [Abstract] [Full Text]  
  • Boor, K. J., Duncan, M. L., Price, C. W. (1995). Genetic and Transcriptional Organization of the Region Encoding the beta Subunit of Bacillus subtilis RNA Polymerase. J. Biol. Chem. 270: 20329-20336 [Abstract] [Full Text]  
  • Weilbaecher, R, Hebron, C, Feng, G, Landick, R (1994). Termination-altering amino acid substitutions in the beta' subunit of Escherichia coli RNA polymerase identify regions involved in RNA chain elongation.. Genes Dev. 8: 2913-2927 [Abstract]  
  • Orlicky, S. M., Tran, P. T., Sayre, M. H., Edwards, A. M. (2001). Dissociable Rpb4-Rpb7 Subassembly of RNA Polymerase II Binds to Single-strand Nucleic Acid and Mediates a Post-recruitment Step in Transcription Initiation. J. Biol. Chem. 276: 10097-10102 [Abstract] [Full Text]  
  • Darst, S. A., Opalka, N., Chacon, P., Polyakov, A., Richter, C., Zhang, G., Wriggers, W. (2002). Conformational flexibility of bacterial RNA polymerase. Proc. Natl. Acad. Sci. USA 99: 4296-4301 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»