Inhibition of human poly(A)-specific ribonuclease (PARN) by purine nucleotides: kinetic analysis

References

• S Meyer, C Temme, and E Wahle. (2004). Messenger RNA turnover in eukaryotes: Pathways and enzymes. Crit Rev Biochem Mol Biol 39:197–216.
   PubMed Web of Science ®Google Scholar
• R Parker, and H Song. (2004). The enzymes and control of eukaryotic mRNA turnover. Nat Struct Mol Biol 11:121–127.
   PubMed Web of Science ®Google Scholar
• AB Sachs, and G Varani. (2000). Eukaryotic translation initiation: There are (at least) two sides to every story. Nat Struct Biol 7:356–361.
   PubMedGoogle Scholar
• AJ Shatkin, and JL Manley. (2000). The ends of the affair: Capping and polyadenylation. Nat Struct Biol 7:838–842.
   PubMedGoogle Scholar
• CJ Wilusz, M Wormington, and SW Peltz. (2001). The cap-to-tail guide to mRNA turnover. Nat Rev Mol Cell Biol 2:237–246.
   PubMed Web of Science ®Google Scholar
• CG Korner, and E Wahle. (1997). Poly (A) tail shortening by a mammalian poly(A)-specific 3′-exoribonuclease. J Biol Chem 272:10448–10456.
   PubMedGoogle Scholar
• J Martinez, YG Ren, AC Thuresson, U Hellman, J Astrom, and A Virtanen. (2000). A 54-kDa fragment of the Poly(A)-specific ribonuclease is an oligomeric, processive, and cap-interacting Poly(A)-specific 3′ exonuclease. J Biol Chem 275:24222–24230.
   PubMedGoogle Scholar
• PR Copeland, and M Wormington. (2001). The mechanism and regulation of deadenylation: Identification and characterization of Xenopus PARN. Rna 7:875–886.
   PubMed Web of Science ®Google Scholar
• SM Varnum, CA Hurney, and WM Wormington. (1992). Maturation-specific deadenylation in Xenopus oocytes requires nuclear and cytoplasmic factors. Dev Biol 153:283–290.
   PubMed Web of Science ®Google Scholar
• J Astrom, A Astrom, and A Virtanen. (1992). Properties of a HeLa cell 3′ exonuclease specific for degrading poly(A) tails of mammalian mRNA. J Biol Chem 267:18154–18159.
   PubMed Web of Science ®Google Scholar
• E Dehlin, M Wormington, CG Korner, and E Wahle. (2000). Cap-dependent deadenylation of mRNA. Embo J 19:1079–1086.
   PubMedGoogle Scholar
• M Gao, DT Fritz, LP Ford, and J Wilusz. (2000). Interaction between a poly(A)-specific ribonuclease and the 5′ cap influences mRNA deadenylation rates in vitro. Mol Cell 5:479–488.
   PubMed Web of Science ®Google Scholar
• J Martinez, YG Ren, P Nilsson, M Ehrenberg, and A Virtanen. (2001). The mRNA cap structure stimulates rate of poly(A) removal and amplifies processivity of degradation. J Biol Chem 276:27923–27929.
   PubMedGoogle Scholar
• M Opyrchal, JR Anderson, KJ Sokoloski, CJ Wilusz, and J Wilusz. (2005). A cell-free mRNA stability assay reveals conservation of the enzymes and mechanisms of mRNA decay between mosquito and mammalian cell lines. Insect Biochem Mol Biol 35:1321–1334.
   PubMedGoogle Scholar
• CG Korner, M Wormington, M Muckenthaler, S Schneider, E Dehlin, and E Wahle. (1998). The deadenylating nuclease (DAN) is involved in poly(A) tail removal during the meiotic maturation of Xenopus oocytes. Embo J 17:5427–5437.
   PubMedGoogle Scholar
• MJ Moser, WR Holley, A Chatterjee, and IS Mian. (1997). The proofreading domain of Escherichia coli DNA polymerase I and other DNA and/or RNA exonuclease domains. Nucleic Acids Res 25:5110–5118.
   PubMed Web of Science ®Google Scholar
• M Wu, M Reuter, H Lilie, Y Liu, E Wahle, and H Song. (2005). Structural insight into poly(A) binding and catalytic mechanism of human PARN. Embo J 24:4082–4093.
   PubMed Web of Science ®Google Scholar
• P Nilsson, N Henriksson, A Niedzwiecka, NA Balatsos, K Kokkoris, J Eriksson, and A Virtanen. (2007). A multifunctional RNA recognition motif (RRM) in poly(A)-specific ribonuclease (PARN) with cap and poly(A) binding properties. J Biol Chem
   Google Scholar
• A Zhang, WF Liu, and YB Yan. (2007). Role of the RRM domain in the activity, structure and stability of poly(A)-specific ribonuclease. Arch Biochem Biophys 461:255–262.
   PubMedGoogle Scholar
• YG Ren, LA Kirsebom, and A Virtanen. (2004). Coordination of divalent metal ions in the active site of poly(A)-specific ribonuclease. J Biol Chem 279:48702–48706.
   PubMedGoogle Scholar
• YG Ren, J Martinez, and A Virtanen. (2002). Identification of the active site of poly(A)-specific ribonuclease by site-directed mutagenesis and Fe(2+)-mediated cleavage. J Biol Chem 277:5982–5987.
   PubMedGoogle Scholar
• P Nilsson, and A Virtanen. (2006). Expression and purification of recombinant poly(A)-specific ribonuclease (PARN). Int J Biol Macromol 39:95–99.
   PubMedGoogle Scholar
• Y Cheng, WF Liu, YB Yan, and HM Zhou. (2006). A nonradioactive assay for poly(a)-specific ribonuclease activity by methylene blue colorimetry. Protein Pept Lett 13:125–128.
   PubMed Web of Science ®Google Scholar
• NA Balatsos, P Nilsson, C Mazza, S Cusack, and A Virtanen. (2006). Inhibition of mRNA deadenylation by the nuclear cap binding complex (CBC). J Biol Chem 281:4517–4522.
   PubMed Web of Science ®Google Scholar
• M Gao, CJ Wilusz, SW Peltz, and J Wilusz. (2001). A novel mRNA-decapping activity in HeLa cytoplasmic extracts is regulated by AU-rich elements. Embo J 20:1134–1143.
   PubMedGoogle Scholar
• R Gherzi, KY Lee, P Briata, D Wegmuller, C Moroni, M Karin, and CY Chen. (2004). A KH domain RNA binding protein, KSRP, promotes ARE-directed mRNA turnover by recruiting the degradation machinery. Mol Cell 14:571–583.
   PubMed Web of Science ®Google Scholar
• WS Lai, EA Kennington, and PJ Blackshear. (2003). Tristetraprolin and its family members can promote the cell-free deadenylation of AU-rich element-containing mRNAs by poly(A) ribonuclease. Mol Cell Biol 23:3798–3812.
   PubMed Web of Science ®Google Scholar
• WJ Lin, A Duffy, and CY Chen. (2007). Localization of AU-rich element-containing mRNA in cytoplasmic granules containing exosome subunits. J Biol Chem 282:19958–19968.
   PubMed Web of Science ®Google Scholar
• KC Moraes, CJ Wilusz, and J Wilusz. (2006). CUG-BP binds to RNA substrates and recruits PARN deadenylase. Rna 12:1084–1091.
   PubMedGoogle Scholar
• R Seal, R Temperley, J Wilusz, RN Lightowlers, and ZM Chrzanowska-Lightowlers. (2005). Serum-deprivation stimulates cap-binding by PARN at the expense of eIF4E, consistent with the observed decrease in mRNA stability. Nucleic Acids Res 33:376–387.
   PubMedGoogle Scholar
• H Tran, M Schilling, C Wirbelauer, D Hess, and Y Nagamine. (2004). Facilitation of mRNA deadenylation and decay by the exosome-bound, DExH protein RHAU. Mol Cell 13:101–111.
   PubMed Web of Science ®Google Scholar
• YG Ren, J Martinez, LA Kirsebom, and A Virtanen. (2002). Inhibition of Klenow DNA polymerase and poly(A)-specific ribonuclease by aminoglycosides. Rna 8:1393–1400.
   PubMedGoogle Scholar
• EM Schwiebert, and A Zsembery. (2003). Extracellular ATP as a signaling molecule for epithelial cells. Biochim Biophys Acta 1615:7–32.
   PubMed Web of Science ®Google Scholar
• NL Garneau, J Wilusz, and CJ Wilusz. (2007). The highways and byways of mRNA decay. Nat Rev Mol Cell Biol 8:113–126.
   PubMed Web of Science ®Google Scholar
• TD Son, M Roux, and M Ellenberger. (1975). Interaction of Mg2+ ions with nucleoside triphosphates by phosphorus magnetic resonance spectroscopy. Nucleic Acids Res 2:1101–1110.
   PubMedGoogle Scholar
• M Cohn, and TR HughesJr. (1962). Nuclear magnetic resonance spectra of adenosine di-and triphosphatetriphosphate. II. Effect of complexing with divalent metal ions. J Biol Chem 237:176–181.
   PubMed Web of Science ®Google Scholar
• F Ramirez, and JF Marecek. (1980). Coordination of magnesium with adenosine 5′-diphosphate and triphosphate. Biochim Biophys Acta 589:21–29.
   PubMedGoogle Scholar
• SL Huang, and MD Tsai. (1982). Does the magnesium(II) ion interact with the alpha-phosphate of adenosine triphosphate? An investigation by oxygen-17 nuclear magnetic resonance. Biochemistry 21:951–959.
   PubMed Web of Science ®Google Scholar
• KB Busch, and H Fromm. (1999). Plant succinic semialdehyde dehydrogenase. Cloning, purification, localization in mitochondria, and regulation by adenine nucleotides. Plant Physiol 121:589–597.
   PubMed Web of Science ®Google Scholar
• CM Galmarini, JR Mackey, and C Dumontet. (2002). Nucleoside analogues and nucleobases in cancer treatment. Lancet Oncol 3:415–424.
   PubMed Web of Science ®Google Scholar