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Structure of the nuclear exosome component Rrp6p reveals an interplay between the active site and the HRDC domain.

Midtgaard SF, Assenholt J, Jonstrup AT, Van LB, Jensen TH, Brodersen DE
Proc Natl Acad Sci U S A 103 11898-903 (2006)
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Cited: 62 times
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Abstract

The multisubunit eukaryotic exosome is an essential RNA processing and degradation machine. In its nuclear form, the exosome associates with the auxiliary factor Rrp6p, which participates in both RNA processing and degradation reactions. The crystal structure of Saccharomyces cerevisiae Rrp6p displays a conserved RNase D core with a flanking HRDC (helicase and RNase D C-terminal) domain in an unusual conformation shown to be important for the processing function of the enzyme. Complexes with AMP and UMP, the products of the RNA degradation process, reveal how the protein specifically recognizes ribonucleotides and their bases. Finally, in vivo mutational studies show the importance of the domain contacts for the processing function of Rrp6p and highlight fundamental differences between the protein and its prokaryotic RNase D counterparts.

Articles - 2hbj mentioned but not cited (4)

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  2. Structure of the nuclear exosome component Rrp6p reveals an interplay between the active site and the HRDC domain. Midtgaard SF, Assenholt J, Jonstrup AT, Van LB, Jensen TH, Brodersen DE. Proc Natl Acad Sci U S A 103 11898-11903 (2006)
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Reviews citing this publication (19)

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Articles citing this publication (39)

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  6. The exosome-binding factors Rrp6 and Rrp47 form a composite surface for recruiting the Mtr4 helicase. Schuch B, Feigenbutz M, Makino DL, Falk S, Basquin C, Mitchell P, Conti E. EMBO J 33 2829-2846 (2014)
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  14. The C-terminal region of the exosome-associated protein Rrp47 is specifically required for box C/D small nucleolar RNA 3'-maturation. Costello JL, Stead JA, Feigenbutz M, Jones RM, Mitchell P. J Biol Chem 286 4535-4543 (2011)
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  16. The Rrp6 C-terminal domain binds RNA and activates the nuclear RNA exosome. Wasmuth EV, Lima CD. Nucleic Acids Res 45 846-860 (2017)
  17. The activity and selectivity of fission yeast Pop2p are affected by a high affinity for Zn2+ and Mn2+ in the active site. Andersen KR, Jonstrup AT, Van LB, Brodersen DE. RNA 15 850-861 (2009)
  18. Structure and function of the regulatory HRDC domain from human Bloom syndrome protein. Kim YM, Choi BS. Nucleic Acids Res 38 7764-7777 (2010)
  19. Perlman syndrome: overgrowth, Wilms tumor predisposition and DIS3L2. Morris MR, Astuti D, Maher ER. Am J Med Genet C Semin Med Genet 163C 106-113 (2013)
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  22. Structure and function of the regulatory C-terminal HRDC domain from Deinococcus radiodurans RecQ. Killoran MP, Keck JL. Nucleic Acids Res 36 3139-3149 (2008)
  23. Poly(A) tail-mediated gene regulation by opposing roles of Nab2 and Pab2 nuclear poly(A)-binding proteins in pre-mRNA decay. Grenier St-Sauveur V, Soucek S, Corbett AH, Bachand F. Mol Cell Biol 33 4718-4731 (2013)
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  32. Substrate selectivity by the exonuclease Rrp6p. Axhemi A, Wasmuth EV, Lima CD, Jankowsky E. Proc Natl Acad Sci U S A 117 982-992 (2020)
  33. Stress-induced nuclear depletion of Entamoeba histolytica 3'-5' exoribonuclease EhRrp6 and its role in growth and erythrophagocytosis. Singh SS, Naiyer S, Bharadwaj R, Kumar A, Singh YP, Ray AK, Subbarao N, Bhattacharya A, Bhattacharya S. J Biol Chem 293 16242-16260 (2018)
  34. Structural analysis of the yeast exosome Rrp6p-Rrp47p complex by small-angle X-ray scattering. Dedic E, Seweryn P, Jonstrup AT, Flygaard RK, Fedosova NU, Hoffmann SV, Boesen T, Brodersen DE. Biochem Biophys Res Commun 450 634-640 (2014)
  35. Characterization of the Catalytic Subunits of the RNA Exosome-like Complex in Plasmodium falciparum. Jiang N, Yu S, Yang N, Feng Y, Sang X, Wang Y, Wahlgren M, Chen Q. J Eukaryot Microbiol 65 843-853 (2018)
  36. Dis3- and exosome subunit-responsive 3' mRNA instability elements. Kiss DL, Hou D, Gross RH, Andrulis ED. Biochem Biophys Res Commun 423 461-466 (2012)
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