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A network of assembly factors is involved in remodeling rRNA elements during preribosome maturation

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  • The following corrections appear in the attached pdf labelled "Correction to Version of Record". The authors inadvertently omitted Woonghee Lee from the list of authors. The corrected author list and affiliations are noted. Revised acknowledgment paragraphs including Woonghee Lee’s funding source and contribution also appear in the correction. In addition, the authors noted the omission of details of NMR structure calculation from the Materials and Methods section. The relevant paragraph and the references associated with it are appended.
  • Eukaryotic ribosome biogenesis involves ∼200 assembly factors, but how these contribute to ribosome maturation is poorly understood. Here, we identify a network of factors on the nascent 60S subunit that actively remodels preribosome structure. At its hub is Rsa4, a direct substrate of the force-generating ATPase Rea1. We show that Rsa4 is connected to the central protuberance by binding to Rpl5 and to ribosomal RNA (rRNA) helix 89 of the nascent peptidyl transferase center (PTC) through Nsa2. Importantly, Nsa2 binds to helix 89 before relocation of helix 89 to the PTC. Structure-based mutations of these factors reveal the functional importance of their interactions for ribosome assembly. Thus, Rsa4 is held tightly in the preribosome and can serve as a “distribution box,” transmitting remodeling energy from Rea1 into the developing ribosome. We suggest that a relay-like factor network coupled to a mechano-enzyme is strategically positioned to relocate rRNA elements during ribosome maturation.
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  • Baßler, J., Paternoga, H., Holdermann, I., Thoms, M., Granneman, S., Barrio-Garcia, C., ... & Hurt, E. (2014). A network of assembly factors is involved in remodeling rRNA elements during preribosome maturation. Journal of Cell Biology, 207(4), 481-498. doi:10.1083/jcb.201408111
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  • 207
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  • 4
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  • J. Baßler and E. Hurt are supported by grants from Deutsche Forschungsgemeinschaft (DFG; BA2316/1-4, HU363/10-5). E. Barbar and A. Nyarko are supported by the National Institutes of Health (GM 084276). I. Sinning acknowledges support by grants from DFG (FOR967, GRK1188, andSFB638). Financial support from the Access to Research Infrastructures activity in the seventh Framework Program of the European Community (Project number 261863, Bio-NMR) for conducting the research is also acknowledged. C. Barrio-Garcia is a fellow of the Graduiertenkolleg GRK 1721.
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file details NyarkoAfuaBiochemBiophyNetworkAssemblyFactors.pdf 10/27/2017 Public
file details J Cell Biol-2015-BaßlerJochenCorrection.pdf 10/27/2017 Public