Cell. 2009 Sep 4;138(5):911-22.

Mechanochemical removal of ribosome biogenesis factors from nascent 60S ribosomal subunits.

Ulbrich C, Diepholz M, Bassler J, Kressler D, Pertschy B, Galani K, Böttcher B, Hurt E.

Source

Biochemie-Zentrum der Universität Heidelberg, Im Neuenheimer Feld 328, 69120 Heidelberg, Germany.

Abstract

The dynein-related AAA ATPase Rea1 is a preribosomal factor that triggers an unknown maturation step in 60S subunit biogenesis. Using electron microscopy, we show that Rea1's motor domain is docked to the pre-60S particle and its tail-like structure, harboring a metal ion-dependent adhesion site (MIDAS), protrudes from the preribosome. Typically, integrins utilize a MIDAS to bind extracellular ligands, an interaction that is strengthened under applied tensile force. Likewise, the Rea1 MIDAS binds the preribosomal factor Rsa4, which is located on the pre-60S subunit at a site that is contacted by the flexible Rea1 tail. The MIDAS-Rsa4 interaction is essential for ATP-dependent dissociation of a group of non-ribosomal factors from the pre-60S particle. Thus, Rea1 aligns with its interacting partners on the preribosome to effect a necessary step on the path to the export-competent 60S subunit.

Comment in

Cell. 2009 Sep 4;138(5):832-4.

PMID:: 19737519; [PubMed - indexed for MEDLINE]

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Cited by 7 PubMed Central articles

The power of AAA-ATPases on the road of pre-60S ribosome maturation - Molecular machines that strip pre-ribosomal particles. [Biochim Biophys Acta. 2012]
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The small subunit processome in ribosome biogenesis—progress and prospects. [Wiley Interdiscip Rev RNA. 2011]
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