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Mpp10 represents a platform for the interaction of multiple factors within the 90S pre-ribosome.

<div class='caption-title'>Assembly factor network and reconstitution of the ctMpp10 module.</div>
<div class='caption-title'>Two hydrophobic patches within the N-terminal region mediate the direct interaction between Mpp10 and Utp3.</div>
<div class='caption-title'>Identification of the minimal Rps5-binding motif within Mpp10.</div>
Sá-Moura B, Kornprobst M, Kharde S, Ahmed YL, Stier G, Kunze R, Sinning I, Hurt E
OpenAccess logo PLoS One 12 e0183272 (2017)
Cited: 11 times
EuropePMC logo PMID: 28813493

Abstract

In eukaryotes, ribosome assembly is a highly complex process that involves more than 200 assembly factors that ensure the folding, modification and processing of the different rRNA species as well as the timely association of ribosomal proteins. One of these factors, Mpp10 associates with Imp3 and Imp4 to form a complex that is essential for the normal production of the 18S rRNA. Here we report the crystal structure of a complex between Imp4 and a short helical element of Mpp10 to a resolution of 1.88 Å. Furthermore, we extend the interaction network of Mpp10 and characterize two novel interactions. Mpp10 is able to bind the ribosome biogenesis factor Utp3/Sas10 through two conserved motifs in its N-terminal region. In addition, Mpp10 interacts with the ribosomal protein S5/uS7 using a short stretch within an acidic loop region. Thus, our findings reveal that Mpp10 provides a platform for the simultaneous interaction with multiple proteins in the 90S pre-ribosome.

Reviews citing this publication (3)

  1. Ribosome assembly coming into focus. Klinge S, Woolford JL. Nat Rev Mol Cell Biol 20 116-131 (2019)
  2. Assembly and structure of the SSU processome-a nucleolar precursor of the small ribosomal subunit. Barandun J, Hunziker M, Klinge S. Curr Opin Struct Biol 49 85-93 (2018)
  3. The Nucleolus: A Multiphase Condensate Balancing Ribosome Synthesis and Translational Capacity in Health, Aging and Ribosomopathies. Correll CC, Bartek J, Dundr M. Cells 8 E869 (2019)

Articles citing this publication (8)

  1. Cryo-EM structure of an early precursor of large ribosomal subunit reveals a half-assembled intermediate. Zhou D, Zhu X, Zheng S, Tan D, Dong MQ, Ye K. Protein Cell 10 120-130 (2019)
  2. Interdependent action of KH domain proteins Krr1 and Dim2 drive the 40S platform assembly. Sturm M, Cheng J, Baßler J, Beckmann R, Hurt E. Nat Commun 8 2213 (2017)
  3. Sas10 controls ribosome biogenesis by stabilizing Mpp10 and delivering the Mpp10-Imp3-Imp4 complex to nucleolus. Zhao S, Chen Y, Chen F, Huang D, Shi H, Lo LJ, Chen J, Peng J. Nucleic Acids Res 47 2996-3012 (2019)
  4. Bud23 promotes the final disassembly of the small subunit Processome in Saccharomyces cerevisiae. Black JJ, Sardana R, Elmir EW, Johnson AW. PLoS Genet 16 e1009215 (2020)
  5. Emergence of the primordial pre-60S from the 90S pre-ribosome. Ismail S, Flemming D, Thoms M, Gomes-Filho JV, Randau L, Beckmann R, Hurt E. Cell Rep 39 110640 (2022)
  6. Functional regions in the 5' external transcribed spacer of yeast pre-rRNA. Chen J, Zhang L, Ye K. RNA 26 866-877 (2020)
  7. Correction: Mpp10 represents a platform for the interaction of multiple factors within the 90S pre-ribosome. Sá-Moura B, Kornprobst M, Kharde S, Ahmed YL, Stier G, Kunze R, Sinning I, Hurt E. PLoS One 15 e0234932 (2020)
  8. Predicted Membrane-Associated Domains in Proteins Encoded by Novel Monopartite Plant RNA Viruses Related to Members of the Family Benyviridae. Morozov SY, Lezzhov AA, Solovyev AG. Int J Mol Sci 24 12161 (2023)


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