Messenger RNA Processing


Principal Investigator
Claire Moore
Professor

Program Affiliations
Biochemistry
Genetics
Molecular Microbiology

Contact Information
Department of Microbiology
Tufts University
136 Harrison Avenue
Boston, MA 02111

Office (617) 636-6935
Lab (617) 636-3645
Fax (617) 636-0337
Email  
Claire.Moore@tufts.edu
  1. Bard, J., Zhelkovsky, A., Helmling, S., Earnest, T., Moore, C., and Bohm, A. (2000) Structure of yeast poly(A) polymerase alone and in complex with 3’dATP. Science 289:1346-1349.
  2. Helmling, S., Zhelkovsky, A., and Moore, C. (2001)  Fip1 regulates the activity of poly(A) polymerase through multiple interactions. Mol. Cell Biol.  21:2026-2037.
  3. Gross, S. and Moore, C. (2001) Five subunits are required for reconstitution of the cleavage and polyadenylation  activities of S. cerevisiae Cleavage Factor 1.  Proc. Nat. Acad. Sci. 98:6080-6085.
  4. Gross, S. and Moore, C. (2001) Rna15 interaction with the A-rich yeast polyadenylation signal is an essential step in mRNA 3’-end formation. Mol. Cell Biol.21:8045-8055.
  5. Hammell, C., Gross, S., Zenklusen, D., Heath, C., Stutz, F., Moore, C., and Cole, C.  (2002) Coupling of termination, 3’ processing and mRNA export.  Mol. Cell. Biol. 22:6441-6457.
  6. Tacahashi, Y., Helmling, S., and Moore, C.  (2003) Functional dissection of the zinc finger and flanking domains of the Yth1 cleavage/polyadenylation factor.  Nucleic Acids Research 31:1-9.
  7. He, X., Khan, A., Cheng, H., Pappas, D., Hampsey, M., & Moore, C. (2003) Functional interactions between transcription and mRNA 3’ end processing machineries mediated by Ssu72 and Sub1. Genes & Dev. 17:1030-1042.
  8. Nedea, E., He, X., Kim, M., Pootoolal, J., Zhong, G. Canadien, V., Hughes, T., Buratowski, S., Moore, C., and Greenblatt, J.  (2003) Organization and function of APT, a subcomplex of the yeast cleavage and polyadenylation factor involved in the formation of mRNA and small nucleolar RNA 3'-ends. J. Biol. Chem. 278:33000-33010.
  9. Zhelkovsky, A., Helmling, S., Bohm, A., and Moore, C.  (2004) Mutations in the middle domain of yeast poly(A) polymerase affect interactions with RNA but not ATP. RNA 10:558-564.
  10. Cheng, H., He, X., and Moore, C. (2004) The WD repeat protein Swd2 has dual functions in transcription termination and lysine 4 methylation of histone H3.  Mol. Cell. Biol 24, 2932-2943.
  11. Krishnamurthy, S., He, X., Reyes-Reyes, M., Moore, C., and Hampsey, M.  (2004)  Ssu72 is a novel RNA polymerase II CTD phosphatase. Mol. Cell. 14:387-394.
  12. He, X.,  and Moore, C. (2005) Regulation of yeast mRNA 3' end processing by phosphorylation. Mol Cell. 19:619-629.
  13. Zhelkovsky, A., Tacahashi, Y., Nasser, T., He, X., Sterzer, U., Jensen, T., Domdey, H., and Moore, C.  2006.  The role of the Brr5/Ysh1 C-terminal domain and its homolog, Syc1, in mRNA 3’ end processing in Saccharomyces cerevisiae. RNA 12:435-445.
  14. Kim, M., Vasiljeva, L., Rando, O., Zhelkovsky, A., Moore, C. and Buratowski, S. (2006)  Distinct mechanisms for snoRNA and mRNA termination. Mol. Cell. 24:723-734.
  15. Qu, X, Perez-Canadillas, J.-M., Agrawal, S., De Baecke. J., Cheng, H., Varani, G., and Moore, C.  (2007) The C-terminal domains of vertebrate CstF-64 and its yeast orthologue Rna15 form a new structure critical for mRNA 3’-end processing. J. Biol. Chem. 282:2101-2115.
  16. Bucheli, M., He, H., Kaplan, C., Moore, C., and Buratowski, S.  (2007)  Polyadenylation site choice in yeast is affected by competition between Npl3 and polyadenylation factor CFI. RNA 13:1756-1764.
  17. Deka, P., Bucheli, M., Moore, C., Buratowski, S., and Varani, G. (2007)  Structure of the yeast SR protein Npl3 and interaction with mRNA 3’-end processing signals. Journal of Molecular Biology 375:136-150.
  18. Saguez, C., Schmid, M., Olesen, J., Ghazy, M., Qu, X., Poulsen, M., Nasser, T., Moore, C., and Jensen, T. (2008)  Nuclear mRNA surveillance in THO/sub2 mutants is triggered by inefficient polyadenylation. Mol.Cell  31:91-103.
  19. Meinke, G., Ezeokokwo, C., Balbo, P., Moore, C., and Bohm.  (2008) Structure of yeast poly(A) polymerase in complex with the polymerase-binding domain of Fip1. Biochemistry. 47:6859-69
  20. Dermody, J., Dreyfuss, J., Villén, J., Ogundipe, B., Gygi, S., Park, P., Ponticelli, A., Moore, C., Buratowski, S. and Bucheli, M. (2008) Phosphorylation regulates novel stimulation of RNA Polymerase II elongation by the SR-like protein Npl3. PLOS one 3:e3273.