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Ribosomal Proteins: Role in Ribosomal Functions

  1. Daniel N Wilson1,
  2. Romi Gupta2,
  3. Aleksandra Mikolajka1,
  4. Knud H Nierhaus2

Published Online: 15 SEP 2009

DOI: 10.1002/9780470015902.a0000687.pub3



How to Cite

Wilson, D. N., Gupta, R., Mikolajka, A. and Nierhaus, K. H. 2009. Ribosomal Proteins: Role in Ribosomal Functions. eLS. .

Author Information

  1. 1

    University of Munich, Munich, Germany

  2. 2

    Max-Planck Institute for Molecular Genetics, Berlin, Germany

Publication History

  1. Published Online: 15 SEP 2009

This is not the most recent version of the article. View current version (15 JUN 2015)


The assignment of specific ribosomal functions to individual ribosomal proteins is difficult due to the enormous cooperativity of the ribosome; however, important roles for distinct ribosomal proteins are becoming evident. Although ribosomal ribonucleic acid (rRNA) has the major claim to certain aspects of ribosome function, such as decoding and peptidyltransferase activity, there are also protein-dominated functional hot-spots on the ribosome such as the messenger RNA (mRNA) entry pore, the translation factor-binding site and the exit of the ribosomal tunnel. The latter is binding site for both chaperones and complexes associated with protein transport through membranes. Furthermore, the contribution of ribosomal proteins is essential for the assembly and optimal functioning of the ribosome.

Key concepts:

Both the 16S and 23S rRNAs and a subset of r-proteins are essential for assembly, structure and function of ribosomes; the ribosomal interface, the place where the three tRNA-binding sites A, P and E are located and thus where protein synthesis occurs, is preferentially composed of rRNA; functional hot-spots such as mRNA entry pore, elongation factor-binding site (L7/L12 stalk), the L1 protuberance and the tunnel exit are dominated by r-proteins; many r-proteins have a globular domain and long extensions protruding deep into the ribosome; the globular domains of r-proteins are located at or near the ribosomal surface; antibiotic resistance can be mediated by mutations in either rRNA or r-protein genes; some r-proteins are essential for assembly but play no role in structure or function of the ribosome; accuracy of proteins is tuned and balanced by r-proteins (S4, S5 and S12); r-proteins at the tunnel exit can function as a docking station for factors important for protein folding or for attaching the ribosome to membranes.


  • rRNA-binding proteins;
  • translational regulation;
  • antitermination;
  • antibiotic resistance;
  • mutant proteins;
  • binding of translational factors