Visualizing ribosome biogenesis: Parallel assembly pathways for the 30S subunit

Anke M. Mulder, Craig Yoshioka, Andrea H. Beck, Anne E. Bunner, Ronald A. Milligan, Clinton S. Potter, Bridget Carragher, James R. Williamson

Research output: Contribution to journalArticlepeer-review

161 Scopus citations


Ribosomes are self-assembling macromolecular machines that translate DNA into proteins, and an understanding of ribosome biogenesis is central to cellular physiology. Previous studies on the Escherichia coli 30S subunit suggest that ribosome assembly occurs via multiple parallel pathways rather than through a single rate-limiting step, but little mechanistic information is known about this process. Discovery single-particle profiling (DSP), an application of time-resolved electron microscopy, was used to obtain more than 1 million snapshots of assembling 30S subunits, identify and visualize the structures of 14 assembly intermediates, and monitor the population flux of these intermediates over time. DSP results were integrated with mass spectrometry data to construct the first ribosome-assembly mechanism that incorporates binding dependencies, rate constants, and structural characterization of populated intermediates.

Original languageEnglish (US)
Pages (from-to)673-677
Number of pages5
Issue number6004
StatePublished - Oct 29 2010
Externally publishedYes

ASJC Scopus subject areas

  • General


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