Int. J. Mol. Sci. 2009, 10(3), 817-834; doi:10.3390/ijms10030817
Review

The Role of Disordered Ribosomal Protein Extensions in the Early Steps of Eubacterial 50 S Ribosomal Subunit Assembly

1 Laboratoire de Cristallographie, Institut de Biologie Physico-Chimique CNRS, 13, rue Pierre et Marie Curie, 75005 Paris, France 2 Laboratoire de Biochimie, Institut de Biologie Physico-Chimique CNRS, 13, rue Pierre et Marie Curie, 75005 Paris, France
* Author to whom correspondence should be addressed.
Received: 5 February 2009; in revised form: 23 February 2009 / Accepted: 24 February 2009 / Published: 2 March 2009
(This article belongs to the Special Issue Protein Folding)
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Abstract: Although during the past decade research has shown the functional importance of disorder in proteins, many of the structural and dynamics properties of intrinsically unstructured proteins (IUPs) remain to be elucidated. This review is focused on the role of the extensions of the ribosomal proteins in the early steps of the assembly of the eubacterial 50 S subunit. The recent crystallographic structures of the ribosomal particles have revealed the picture of a complex assembly pathway that condenses the rRNA and the ribosomal proteins into active ribosomes. However, little is know about the molecular mechanisms of this process. It is thought that the long basic r-protein extensions that penetrate deeply into the subunit cores play a key role through disorder-order transitions and/or co-folding mechanisms. A current view is that such structural transitions may facilitate the proper rRNA folding. In this paper, the structures of the proteins L3, L4, L13, L20, L22 and L24 that have been experimentally found to be essential for the first steps of ribosome assembly have been compared. On the basis of their structural and dynamics properties, three categories of extensions have been identified. Each of them seems to play a distinct function. Among them, only the coil-helix transition that occurs in a phylogenetically conserved cluster of basic residues of the L20 extension appears to be strictly required for the large subunit assembly in eubacteria. The role of a helix-coil transitions in 23 S RNA folding is discussed in the light of the calcium binding protein calmodulin that shares many structural and dynamics properties with L20.
Keywords: Flexibility; structural transitions; helix-coil; calmodulin; linker; electrostatic; helix unwinding; unfolding

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MDPI and ACS Style

Timsit, Y.; Acosta, Z.; Allemand, F.; Chiaruttini, C.; Springer, M. The Role of Disordered Ribosomal Protein Extensions in the Early Steps of Eubacterial 50 S Ribosomal Subunit Assembly. Int. J. Mol. Sci. 2009, 10, 817-834.

AMA Style

Timsit Y, Acosta Z, Allemand F, Chiaruttini C, Springer M. The Role of Disordered Ribosomal Protein Extensions in the Early Steps of Eubacterial 50 S Ribosomal Subunit Assembly. International Journal of Molecular Sciences. 2009; 10(3):817-834.

Chicago/Turabian Style

Timsit, Youri; Acosta, Zahir; Allemand, Frédéric; Chiaruttini, Claude; Springer, Mathias. 2009. "The Role of Disordered Ribosomal Protein Extensions in the Early Steps of Eubacterial 50 S Ribosomal Subunit Assembly." Int. J. Mol. Sci. 10, no. 3: 817-834.

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