the role of disordered ribosomal protein extensions in the early steps of eubacterial 50 s ribosomal subunit assembly无序核糖体蛋白的作用扩展步骤eubacterial 50年代初核糖体亚基组装.pdfVIP

Int. J. Mol. Sci. 2009, 10, 817-834; doi:10.3390/ijm OPEN ACCESS International Journal of Molecular Sciences ISSN 1422-0067 /journal/ijms Review The Role of Disordered Ribosomal Protein Extensions in the Early Steps of Eubacterial 50 S Ribosomal Subunit Assembly Youri Timsit 1,*, Zahir Acosta 1, Frédéric Allemand 2, Claude Chiaruttini 2 and 2 Mathias Springer 1 Laboratoire de Cristallographie, Institut de Biologie Physico-Chimique CNRS, 13, rue Pierre et Marie Curie, 75005 Paris, France; E-Mail: zahiracosta@ 2 Laboratoire de Biochimie, Institut de Biologie Physico-Chimique CNRS, 13, rue Pierre et Marie Curie, 75005 Paris, France; E-Mail: frederic.allemand@ibpc.fr (F.A.); claude.chiaruttini@ibpc.fr (C.C.); Mathias.Springer@ibpc.fr (M.S.) * Author to whom correspondence should be addressed; E-mail: timsit@ibpc.fr; Tel. +01-58-41-51-66 Received: 5 February 2009; in revised form: 23 February 2009 / Accepted: 24 February 2009 / Published: 2 March 2009 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 structu