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Nucleic Acids Research Advance Access published online on September 29, 2009
Nucleic Acids Research, doi:10.1093/nar/gkp806
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© The Author(s) 2009. Published by Oxford University Press.
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.5/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Molecular Biology

Role and dynamics of the ribosomal protein P0 and its related trans-acting factor Mrt4 during ribosome assembly in Saccharomyces cerevisiae

María Rodríguez-Mateos1, Juan J. García-Gómez2, Rosario Francisco-Velilla1, Miguel Remacha1, Jesús de la Cruz2 and Juan P. G. Ballesta1,*

1Centro de Biología Molecular Severo Ochoa, Consejo Superior de Investigaciones Científicas and Universidad Autónoma de Madrid, Cantoblanco E-28049 Madrid and 2Departamento de Genética, Universidad de Sevilla, E-41012 Sevilla, Spain

*To whom correspondence should be addressed. Tel: +34 911964505; Fax: +34 911964420; Email: jpgballesta{at}cbm.uam.es Correspondence may also be addressed to Jesús de la Cruz. Tel: +34 954557106; Fax: +34 954557104; Email: jdlcd{at}us.es

Received July 15, 2009. Revised September 8, 2009. Accepted September 11, 2009.

Mrt4 is a nucleolar component of the ribosome assembly machinery that shares notable similarity and competes for binding to the 25S rRNA GAR domain with the ribosomal protein P0. Here, we show that loss of function of either P0 or Mrt4 results in a deficit in 60S subunits, which is apparently due to impaired rRNA processing of 27S precursors. Mrt4, which shuttles between the nucleus and the cytoplasm, defines medium pre-60S particles. In contrast, P0 is absent from medium but present in late/cytoplasmic pre-60S complexes. The absence of Mrt4 notably increased the amount of P0 in nuclear Nop7–TAP complexes and causes P0 assembly to medium pre-60S particles. Upon P0 depletion, Mrt4 is relocated to the cytoplasm within aberrant 60S subunits. We conclude that Mrt4 controls the position and timing of P0 assembly. In turn, P0 is required for the release of Mrt4 and exchanges with this factor at the cytoplasm. Our results also suggest other P0 assembly alternatives.

The authors wish it to be known that, in their opinion, the first two authors should be regarded as joint First Authors.


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