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Structural basis of m(7)GpppG binding to poly(A)-specific ribonuclease.

Wu M, Nilsson P, Henriksson N, Niedzwiecka A, Lim MK, Cheng Z, Kokkoris K, Virtanen A, Song H
Structure 17 276-86 (2009)
Cited: 40 times
EuropePMC logo PMID: 19217398

Abstract

Poly(A)-specific ribonuclease (PARN) is a homodimeric, processive, and cap-interacting 3' exoribonuclease that efficiently degrades eukaryotic mRNA poly(A) tails. The crystal structure of a C-terminally truncated PARN in complex with m(7)GpppG reveals that, in one subunit, m(7)GpppG binds to a cavity formed by the RRM domain and the nuclease domain, whereas in the other subunit, it binds almost exclusively to the RRM domain. Importantly, our structural and competition data show that the cap-binding site overlaps with the active site in the nuclease domain. Mutational analysis demonstrates that residues involved in m(7)G recognition are crucial for cap-stimulated deadenylation activity, and those involved in both cap and poly(A) binding are important for catalysis. A modeled PARN, which shows that the RRM domain from one subunit and the R3H domain from the other subunit enclose the active site, provides a structural foundation for further studies to elucidate the mechanism of PARN-mediated deadenylation.

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Reviews citing this publication (13)

  1. Cap and cap-binding proteins in the control of gene expression. Topisirovic I, Svitkin YV, Sonenberg N, Shatkin AJ. Wiley Interdiscip Rev RNA 2 277-298 (2011)
  2. Cap-binding complex (CBC). Gonatopoulos-Pournatzis T, Cowling VH. Biochem J 457 231-242 (2014)
  3. Molecular basis of telomere dysfunction in human genetic diseases. Sarek G, Marzec P, Margalef P, Boulton SJ. Nat Struct Mol Biol 22 867-874 (2015)
  4. Cytoplasmic deadenylation: regulation of mRNA fate. Wiederhold K, Passmore LA. Biochem Soc Trans 38 1531-1536 (2010)
  5. Poly(A)-specific ribonuclease (PARN): an allosterically regulated, processive and mRNA cap-interacting deadenylase. Virtanen A, Henriksson N, Nilsson P, Nissbeck M. Crit Rev Biochem Mol Biol 48 192-209 (2013)
  6. RNA-modifying proteins as anticancer drug targets. Boriack-Sjodin PA, Ribich S, Copeland RA. Nat Rev Drug Discov 17 435-453 (2018)
  7. Intracellular ribonucleases involved in transcript processing and decay: precision tools for RNA. Arraiano CM, Mauxion F, Viegas SC, Matos RG, Séraphin B. Biochim Biophys Acta 1829 491-513 (2013)
  8. Deadenylation: enzymes, regulation, and functional implications. Yan YB. Wiley Interdiscip Rev RNA 5 421-443 (2014)
  9. Kiss your tail goodbye: the role of PARN, Nocturnin, and Angel deadenylases in mRNA biology. Godwin AR, Kojima S, Green CB, Wilusz J. Biochim Biophys Acta 1829 571-579 (2013)
  10. Dissimilar roles of the four conserved acidic residues in the thermal stability of poly(A)-specific ribonuclease. He GJ, Liu WF, Yan YB. Int J Mol Sci 12 2901-2916 (2011)
  11. FXR1a-associated microRNP: A driver of specialized non-canonical translation in quiescent conditions. Bukhari SI, Vasudevan S. RNA Biol 14 137-145 (2017)
  12. Translation Initiation Regulated by RNA-Binding Protein in Mammals: The Modulation of Translation Initiation Complex by Trans-Acting Factors. Fukao A, Tomohiro T, Fujiwara T. Cells 10 1711 (2021)
  13. NCBP3: A Multifaceted Adaptive Regulator of Gene Expression. Rambout X, Maquat LE. Trends Biochem Sci 46 87-96 (2021)

Articles citing this publication (23)



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