Rrp17p Is a Eukaryotic Exonuclease Required for 5′ End Processing of Pre-60S Ribosomal RNA

Marlene Oeffinger, Daniel Zenklusen, Angelica Ferguson, Karen E. Wei, Aziz El Hage, David Tollervey, Brian T. Chait, Robert H. Singer, Michael P. Rout

Research output: Contribution to journalArticle

47 Citations (Scopus)

Abstract

Ribosomal processing requires a series of endo- and exonucleolytic steps for the production of mature ribosomes, of which most have been described. To ensure ribosome synthesis, 3′ end formation of rRNA uses multiple nucleases acting in parallel; however, a similar parallel mechanism had not been described for 5′ end maturation. Here, we identify Rrp17p as a previously unidentified 5′-3′ exonuclease essential for ribosome biogenesis, functioning with Rat1p in a parallel processing pathway analogous to that of 3′ end formation. Rrp17p is required for efficient exonuclease digestion of the mature 5′ ends of 5.8SS and 25S rRNAs, contains a catalytic domain close to its N terminus, and is highly conserved among higher eukaryotes, being a member of a family of exonucleases. We show that Rrp17p binds late pre-60S ribosomes, accompanying them from the nucleolus to the nuclear periphery, and provide evidence for physical and functional links between late 60S subunit processing and export.

Original languageEnglish (US)
Pages (from-to)768-781
Number of pages14
JournalMolecular Cell
Volume36
Issue number5
DOIs
StatePublished - Dec 11 2009

Fingerprint

Phosphodiesterase I
Ribosomal RNA
Ribosomes
Exonucleases
Eukaryota
Digestion
Catalytic Domain

Keywords

  • PROTEINS
  • RNA

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

Cite this

Oeffinger, M., Zenklusen, D., Ferguson, A., Wei, K. E., El Hage, A., Tollervey, D., ... Rout, M. P. (2009). Rrp17p Is a Eukaryotic Exonuclease Required for 5′ End Processing of Pre-60S Ribosomal RNA. Molecular Cell, 36(5), 768-781. https://doi.org/10.1016/j.molcel.2009.11.011

Rrp17p Is a Eukaryotic Exonuclease Required for 5′ End Processing of Pre-60S Ribosomal RNA. / Oeffinger, Marlene; Zenklusen, Daniel; Ferguson, Angelica; Wei, Karen E.; El Hage, Aziz; Tollervey, David; Chait, Brian T.; Singer, Robert H.; Rout, Michael P.

In: Molecular Cell, Vol. 36, No. 5, 11.12.2009, p. 768-781.

Research output: Contribution to journalArticle

Oeffinger, M, Zenklusen, D, Ferguson, A, Wei, KE, El Hage, A, Tollervey, D, Chait, BT, Singer, RH & Rout, MP 2009, 'Rrp17p Is a Eukaryotic Exonuclease Required for 5′ End Processing of Pre-60S Ribosomal RNA', Molecular Cell, vol. 36, no. 5, pp. 768-781. https://doi.org/10.1016/j.molcel.2009.11.011
Oeffinger M, Zenklusen D, Ferguson A, Wei KE, El Hage A, Tollervey D et al. Rrp17p Is a Eukaryotic Exonuclease Required for 5′ End Processing of Pre-60S Ribosomal RNA. Molecular Cell. 2009 Dec 11;36(5):768-781. https://doi.org/10.1016/j.molcel.2009.11.011
Oeffinger, Marlene ; Zenklusen, Daniel ; Ferguson, Angelica ; Wei, Karen E. ; El Hage, Aziz ; Tollervey, David ; Chait, Brian T. ; Singer, Robert H. ; Rout, Michael P. / Rrp17p Is a Eukaryotic Exonuclease Required for 5′ End Processing of Pre-60S Ribosomal RNA. In: Molecular Cell. 2009 ; Vol. 36, No. 5. pp. 768-781.
@article{74096860c91642489a4012beba365837,
title = "Rrp17p Is a Eukaryotic Exonuclease Required for 5′ End Processing of Pre-60S Ribosomal RNA",
abstract = "Ribosomal processing requires a series of endo- and exonucleolytic steps for the production of mature ribosomes, of which most have been described. To ensure ribosome synthesis, 3′ end formation of rRNA uses multiple nucleases acting in parallel; however, a similar parallel mechanism had not been described for 5′ end maturation. Here, we identify Rrp17p as a previously unidentified 5′-3′ exonuclease essential for ribosome biogenesis, functioning with Rat1p in a parallel processing pathway analogous to that of 3′ end formation. Rrp17p is required for efficient exonuclease digestion of the mature 5′ ends of 5.8SS and 25S rRNAs, contains a catalytic domain close to its N terminus, and is highly conserved among higher eukaryotes, being a member of a family of exonucleases. We show that Rrp17p binds late pre-60S ribosomes, accompanying them from the nucleolus to the nuclear periphery, and provide evidence for physical and functional links between late 60S subunit processing and export.",
keywords = "PROTEINS, RNA",
author = "Marlene Oeffinger and Daniel Zenklusen and Angelica Ferguson and Wei, {Karen E.} and {El Hage}, Aziz and David Tollervey and Chait, {Brian T.} and Singer, {Robert H.} and Rout, {Michael P.}",
year = "2009",
month = "12",
day = "11",
doi = "10.1016/j.molcel.2009.11.011",
language = "English (US)",
volume = "36",
pages = "768--781",
journal = "Molecular Cell",
issn = "1097-2765",
publisher = "Cell Press",
number = "5",

}

TY - JOUR

T1 - Rrp17p Is a Eukaryotic Exonuclease Required for 5′ End Processing of Pre-60S Ribosomal RNA

AU - Oeffinger, Marlene

AU - Zenklusen, Daniel

AU - Ferguson, Angelica

AU - Wei, Karen E.

AU - El Hage, Aziz

AU - Tollervey, David

AU - Chait, Brian T.

AU - Singer, Robert H.

AU - Rout, Michael P.

PY - 2009/12/11

Y1 - 2009/12/11

N2 - Ribosomal processing requires a series of endo- and exonucleolytic steps for the production of mature ribosomes, of which most have been described. To ensure ribosome synthesis, 3′ end formation of rRNA uses multiple nucleases acting in parallel; however, a similar parallel mechanism had not been described for 5′ end maturation. Here, we identify Rrp17p as a previously unidentified 5′-3′ exonuclease essential for ribosome biogenesis, functioning with Rat1p in a parallel processing pathway analogous to that of 3′ end formation. Rrp17p is required for efficient exonuclease digestion of the mature 5′ ends of 5.8SS and 25S rRNAs, contains a catalytic domain close to its N terminus, and is highly conserved among higher eukaryotes, being a member of a family of exonucleases. We show that Rrp17p binds late pre-60S ribosomes, accompanying them from the nucleolus to the nuclear periphery, and provide evidence for physical and functional links between late 60S subunit processing and export.

AB - Ribosomal processing requires a series of endo- and exonucleolytic steps for the production of mature ribosomes, of which most have been described. To ensure ribosome synthesis, 3′ end formation of rRNA uses multiple nucleases acting in parallel; however, a similar parallel mechanism had not been described for 5′ end maturation. Here, we identify Rrp17p as a previously unidentified 5′-3′ exonuclease essential for ribosome biogenesis, functioning with Rat1p in a parallel processing pathway analogous to that of 3′ end formation. Rrp17p is required for efficient exonuclease digestion of the mature 5′ ends of 5.8SS and 25S rRNAs, contains a catalytic domain close to its N terminus, and is highly conserved among higher eukaryotes, being a member of a family of exonucleases. We show that Rrp17p binds late pre-60S ribosomes, accompanying them from the nucleolus to the nuclear periphery, and provide evidence for physical and functional links between late 60S subunit processing and export.

KW - PROTEINS

KW - RNA

UR - http://www.scopus.com/inward/record.url?scp=71149112138&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=71149112138&partnerID=8YFLogxK

U2 - 10.1016/j.molcel.2009.11.011

DO - 10.1016/j.molcel.2009.11.011

M3 - Article

C2 - 20005841

AN - SCOPUS:71149112138

VL - 36

SP - 768

EP - 781

JO - Molecular Cell

JF - Molecular Cell

SN - 1097-2765

IS - 5

ER -