TY - JOUR
T1 - Visualizing ribosome biogenesis
T2 - Parallel assembly pathways for the 30S subunit
AU - Mulder, Anke M.
AU - Yoshioka, Craig
AU - Beck, Andrea H.
AU - Bunner, Anne E.
AU - Milligan, Ronald A.
AU - Potter, Clinton S.
AU - Carragher, Bridget
AU - Williamson, James R.
N1 - Copyright:
Copyright 2011 Elsevier B.V., All rights reserved.
PY - 2010/10/29
Y1 - 2010/10/29
N2 - 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.
AB - 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.
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U2 - 10.1126/science.1193220
DO - 10.1126/science.1193220
M3 - Article
C2 - 21030658
AN - SCOPUS:78049406997
SN - 0036-8075
VL - 330
SP - 673
EP - 677
JO - Science
JF - Science
IS - 6004
ER -