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GTP-dependent formation of a ribonucleoprotein subcomplex required for ribosome biogenesis

Academic Article
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Overview

authors

  • Karbstein, Katrin
  • Doudna, J. A.

publication date

  • February 2006

journal

  • Journal of Molecular Biology  Journal

abstract

  • Ribosome biogenesis in eukaryotic organisms involves the coordinated assembly of 78 ribosomal proteins onto the four ribosomal RNAs, mediated by a host of trans-acting factors whose specific functions remain largely unknown. The essential GTPase Bms1, the putative endonuclease Rcl1 and the essential U3 small nucleolar RNA form a stable subcomplex thought to control an early step in the assembly of the 40S ribosomal subunit. Here, we provide a complete thermodynamic analysis of GTP-dependent subcomplex formation, revealing strong thermodynamic coupling of Rcl1, U3 small nucleolar RNA and GTP binding to Bms1 that is eliminated in the presence of GDP. The results suggest that Rcl1 activates Bms1 by promoting GDP/GTP exchange, analogous to ribosome-promoted nucleotide exchange within translation elongation factor EF-G. These and other data unveil thermodynamic similarities between Bms1 and the subgroup of GTPases involved in translation, providing evidence that parts of the ribosome assembly machinery may have evolved from the translation apparatus. This quantitative description of an early and essential step in pre-ribosome assembly provides a framework for elucidating the network of interactions between the Bms1 subcomplex and additional factors involved in ribosome biogenesis.

subject areas

  • GTP-Binding Proteins
  • Guanosine Diphosphate
  • Guanosine Triphosphate
  • Guanylyl Imidodiphosphate
  • Macromolecular Substances
  • Nuclear Proteins
  • Protein Binding
  • RNA, Small Nucleolar
  • RNA-Binding Proteins
  • Ribonucleoproteins
  • Ribosomes
  • Saccharomyces cerevisiae Proteins
  • Thermodynamics
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Research

keywords

  • GTPase
  • RNA
  • pre-ribosome assembly
  • ribosome
  • ribosome biogenesis
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Identity

International Standard Serial Number (ISSN)

  • 0022-2836

Digital Object Identifier (DOI)

  • 10.1016/j.jmb.2005.11.052

PubMed ID

  • 16376378
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Additional Document Info

start page

  • 432

end page

  • 443

volume

  • 356

issue

  • 2

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