Article abstract

Nature Structural & Molecular Biology 16, 274 - 280 (2009)
Published online: 8 February 2009 | doi:10.1038/nsmb.1554

Transient ribosomal attenuation coordinates protein synthesis and co-translational folding

Gong Zhang1,2, Magdalena Hubalewska1 & Zoya Ignatova1,2

Clustered codons that pair to low-abundance tRNA isoacceptors can form slow-translating regions in the mRNA and cause transient ribosomal arrest. We report that folding efficiency of the Escherichia coli multidomain protein SufI can be severely perturbed by alterations in ribosome-mediated translational attenuation. Such alterations were achieved by global acceleration of the translation rate with tRNA excess in vitro or by synonymous substitutions to codons with highly abundant tRNAs both in vitro and in vivo. Conversely, the global slow-down of the translation rate modulated by low temperature suppresses the deleterious effect of the altered translational attenuation pattern. We propose that local discontinuous translation temporally separates the translation of segments of the peptide chain and actively coordinates their co-translational folding.

  1. Department of Cellular Biochemistry, Max-Planck-Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany.
  2. Department of Biochemistry, Institute of Biochemistry and Biology, University of Potsdam, Karl-Liebknecht-Str 24-25, 14476 Potsdam-Golm, Germany.

Correspondence to: Zoya Ignatova1,2 e-mail: