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  • The EMBO Journal (2000) 19, 489 - 495
  • doi:10.1093/emboj/19.4.489

Macromolecular mimicry

Poul Nissen1,2, Morten Kjeldgaard1 and Jens Nyborg1

  1. Institute of Molecular and Structural Biology, University of Aarhus, Gustav Wieds vej 10C, DK-8000 Aarhus C, Denmark
  2. Permanent address: Department of Molecular Biophysics and Biochemistry, Yale University, Bass Center 421, 266 Whitney Avenue, PO Box 208114, New Haven, CT 06520-8114, USA

Correspondence to:

Jens Nyborg, E-mail: jnb@imsb.au.dk

Received 18 October 1999; Accepted 8 December 1999; Revised 3 December 1999

Some proteins have been shown to mimic the overall shape and structure of nucleic acids. For some of the proteins involved in translating the genetic information into proteins on the ribosome particle, there are indications that such observations of macromolecular mimicry even extend to similarity in interaction with and function on the ribosome. A small number of structural results obtained outside the protein biosynthesis machinery could indicate that the concept of macromolecular mimicry between proteins and nucleic acids is more general. The implications for the function and evolution of protein biosynthesis are discussed.

  • Keywords:

    • elongation factor G,
    • elongation factor Tu,
    • protein–nucleic acid interactions,
    • ribosomal function,
    • RNA world