Mutations in the middle domain of yeast poly(A) polymerase affect interactions with RNA but not ATP

RNA

Volumn 10, Issue 4, 2004, Pages 558-564

  Zhelkovsky, Alexander ^a   Helmling, Steffen ^b   Bohm, Andrew ^a   Moore, Claire ^a  

^a TUFTS UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b NOXXON PHARMA AG   (Germany)

Author keywords

Nucleotidyl transferase; Poly(A) polymerase; Polyadenylation

Indexed keywords

ADENOSINE TRIPHOSPHATE; MUTANT PROTEIN; NUCLEOTIDYLTRANSFERASE; POLYNUCLEOTIDE ADENYLYLTRANSFERASE; POLYNUCLEOTIDE ADENYLYLTRANSFERASE 1; RNA; UNCLASSIFIED DRUG;

ARTICLE; ENZYME STRUCTURE; ENZYME SUBSTRATE; EUKARYOTIC CELL; NONHUMAN; POLYADENYLATION; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; STRUCTURE ANALYSIS; THREE DIMENSIONAL IMAGING; YEAST;

ADENOSINE TRIPHOSPHATE; ANIMALS; BINDING SITES; CATTLE; MUTATION; POLYNUCLEOTIDE ADENYLYLTRANSFERASE; PROTEIN STRUCTURE, TERTIARY; RNA; YEASTS;

BOVINAE; EUKARYOTA;

EID: 1642488298     PISSN: 13558382     EISSN: None     Source Type: Journal    
DOI: 10.1261/rna.5238704     Document Type: Article

References (16)

1. Astatke, M., Grindley, N.D., and Joyce, C.M. 1995. Deoxynucleoside triphosphate and pyrophosphate binding sites in the catalytically competent ternary complex for the polymerase reaction catalyzed by DNA polymerase I (Klenow fragment). J. Biol. Chem. 270: 1945-1954.
2. 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′-deoxyATP. Science 289: 1346-1349.
3. Delarue, M., Boule, J.B., Lescar, J., Expert-Bezancon, N., Jourdan, N., Sukumar, N., Rougeon, F., and Papanicolaou, C. 2002. Crystal structures of a template-independent DNA polymerase: Murine terminal deoxynucleotidyltransferase. EMBO J. 21: 427-439.
4. Doublie, S., Sawaya, M.R., and Ellenberger, T. 1999. An open and closed case for all polymerases. Structure Fold Des. 7: R31-35.
5. Edmonds, M. 2002. A history of poly A sequences: From formation to factors to function. Prog. Nucleic Acid Res. Mol. Biol. 71: 285-389.
6. Helmling, S., Zhelkovsky, A., and Moore, C.L. 2001. Fip1 regulates the activity of poly(A) polymerase through multiple interactions. Mol. Cell. Biol. 21: 2026-2037.
7. Holm, L. and Sander, C. 1995. DNA polymerase β belongs to an ancient nucleotidyltransferase superfamily. Trends Biochem. Sci. 20: 345-347.
8. Lingner, J., Kellermann, J., and Keller, W. 1991. Cloning and expression of the essential gene for poly(A) polymerase from S. cerevisiae. Nature 354: 496-498.
9. Martin, G., Jeno, P., and Keller, W. 1999. Mapping of ATP binding regions in poly(A) polymerases by photoaffinity labeling and by mutational analysis identifies a domain conserved in many nucleotidyltransferases. Protein Sci. 8: 2380-2391.
10. Martin, G., Keller, W., and Doublie, S. 2000. Crystal structure of mammalian poly(A) polymerase in complex with an analog of ATP. EMBO J. 19: 4193-4203.
11. Sousa, R. and Padilla, R. 1995. A mutant T7 RNA polymerase as a DNA polymerase. EMBO J. 14: 4609-4621.
12. Studier, F.W., Rosenberg, A.H., Dunn, J.J., and Dubendorff, J.W. 1990. Use of T7 RNA polymerase to direct expression of cloned genes. Methods Enzymol. 185: 60-89.
13. Yue, D., Maizels, N., and Weiner, A.M. 1996. CCA-adding enzymes and poly(A) polymerases are all members of the same nucleotidyltransferase superfamily: Characterization of the CCA-adding enzyme from the archael hyperthermophile Sulfolobus shibatae. RNA 2: 895-908.
14. Zhao, J., Hyman, L., and Moore, C. 1999. Formation of mRNA 3′ ends in eukaryotes: Mechanism, regulation and interrelationships with other steps in mRNA synthesis. Microbiol. Mol. Biol. Rev. 63: 405-445.
15. Zhelkovsky, A.M., Kessler, M.M., and Moore, C.L. 1995. Structure-function relationships in the Saccharomyces cerevisiae poly(A) polymerase. J. Biol. Chem. 270: 26715-26720.
16. Zhelkovsky, A., Helmling, S., and Moore, C. 1998. Processivity of the Saccharomyces cerevisiae poly(A) polymerase requires interactions at the carboxyl-terminal RNA binding domain. Mol. Cell. Biol. 18: 5942-5951.