This Article
Right arrow Full Text
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 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 Mangus, D. A.
Right arrow Articles by Jacobson, A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Mangus, D. A.
Right arrow Articles by Jacobson, A.

 Previous Article  |  Next Article 

Molecular and Cellular Biology, June 2004, p. 5521-5533, Vol. 24, No. 12
0270-7306/04/$08.00+0     DOI: 10.1128/MCB.24.12.5521-5533.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Positive and Negative Regulation of Poly(A) Nuclease

David A. Mangus, Matthew C. Evans, Nathan S. Agrin, Mandy Smith, Preetam Gongidi,{dagger}, and Allan Jacobson*

Department of Molecular Genetics and Microbiology University of Massachusetts Medical School, Worcester, Massachusetts 01655

Received 26 September 2003/ Returned for modification 4 November 2003/ Accepted 17 March 2004

PAN, a yeast poly(A) nuclease, plays an important nuclear role in the posttranscriptional maturation of mRNA poly(A) tails. The activity of this enzyme is dependent on its Pan2p and Pan3p subunits, as well as the presence of poly(A)-binding protein (Pab1p). We have identified and characterized the associated network of factors controlling the maturation of mRNA poly(A) tails in yeast and defined its relevant protein-protein interactions. Pan3p, a positive regulator of PAN activity, interacts with Pab1p, thus providing substrate specificity for this nuclease. Pab1p also regulates poly(A) tail trimming by interacting with Pbp1p, a factor that appears to negatively regulate PAN. Pan3p and Pbp1p both interact with themselves and with the C terminus of Pab1p. However, the domains required for Pan3p and Pbp1p binding on Pab1p are distinct. Single amino acid changes that disrupt Pan3p interaction with Pab1p have been identified and define a binding pocket in helices 2 and 3 of Pab1p's carboxy terminus. The importance of these amino acids for Pab1p-Pan3p interaction, and poly(A) tail regulation, is underscored by experiments demonstrating that strains harboring substitutions in these residues accumulate mRNAs with long poly(A) tails in vivo.

* Corresponding author. Mailing address: Department of Molecular Genetics and Microbiology, University of Massachusetts Medical School, Worcester, MA 01655. Phone: (508) 856-2442. Fax: (508) 856-5920. E-mail: allan.jacobson{at}umassmed.edu.

{dagger} Present address: Program in Molecular Biology and Biotechnology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599.

Molecular and Cellular Biology, June 2004, p. 5521-5533, Vol. 24, No. 12
0022-538X/04/$08.00+0     DOI: 10.1128/MCB.24.12.5521-5533.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Zheng, D., Ezzeddine, N., Chen, C.-Y. A., Zhu, W., He, X., Shyu, A.-B. (2008). Deadenylation is prerequisite for P-body formation and mRNA decay in mammalian cells. JCB 182: 89-101 [Abstract] [Full Text]  
  • Funakoshi, Y., Doi, Y., Hosoda, N., Uchida, N., Osawa, M., Shimada, I., Tsujimoto, M., Suzuki, T., Katada, T., Hoshino, S.-i. (2007). Mechanism of mRNA deadenylation: evidence for a molecular interplay between translation termination factor eRF3 and mRNA deadenylases. Genes Dev. 21: 3135-3148 [Abstract] [Full Text]  
  • Simon, E., Seraphin, B. (2007). A specific role for the C-terminal region of the Poly(A)-binding protein in mRNA decay. Nucleic Acids Res 35: 6017-6028 [Abstract] [Full Text]  
  • Yao, G., Chiang, Y.-C., Zhang, C., Lee, D. J., Laue, T. M., Denis, C. L. (2007). PAB1 Self-Association Precludes Its Binding to Poly(A), Thereby Accelerating CCR4 Deadenylation In Vivo. Mol. Cell. Biol. 27: 6243-6253 [Abstract] [Full Text]  
  • Siddiqui, N., Mangus, D. A., Chang, T.-C., Palermino, J.-M., Shyu, A.-B., Gehring, K. (2007). Poly(A) Nuclease Interacts with the C-terminal Domain of Polyadenylate-binding Protein Domain from Poly(A)-binding Protein. J. Biol. Chem. 282: 25067-25075 [Abstract] [Full Text]  
  • Perreault, A., Lemieux, C., Bachand, F. (2007). Regulation of the Nuclear Poly(A)-binding Protein by Arginine Methylation in Fission Yeast. J. Biol. Chem. 282: 7552-7562 [Abstract] [Full Text]  
  • Noble, C. G., Beuth, B., Taylor, I. A. (2007). Structure of a nucleotide-bound Clp1-Pcf11 polyadenylation factor. Nucleic Acids Res 35: 87-99 [Abstract] [Full Text]  
  • Keeling, K. M., Salas-Marco, J., Osherovich, L. Z., Bedwell, D. M. (2006). Tpa1p Is Part of an mRNP Complex That Influences Translation Termination, mRNA Deadenylation, and mRNA Turnover in Saccharomyces cerevisiae.. Mol. Cell. Biol. 26: 5237-5248 [Abstract] [Full Text]  
  • Hosoda, N., Lejeune, F., Maquat, L. E. (2006). Evidence that Poly(A) Binding Protein C1 Binds Nuclear Pre-mRNA Poly(A) Tails. Mol. Cell. Biol. 26: 3085-3097 [Abstract] [Full Text]  
  • Dheur, S., Nykamp, K. R., Viphakone, N., Swanson, M. S., Minvielle-Sebastia, L. (2005). Yeast mRNA Poly(A) Tail Length Control Can Be Reconstituted in Vitro in the Absence of Pab1p-dependent Poly(A) Nuclease Activity. J. Biol. Chem. 280: 24532-24538 [Abstract] [Full Text]  
  • Dunn, E. F., Hammell, C. M., Hodge, C. A., Cole, C. N. (2005). Yeast poly(A)-binding protein, Pab1, and PAN, a poly(A) nuclease complex recruited by Pab1, connect mRNA biogenesis to export. Genes Dev. 19: 90-103 [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»