Visualizing Ribosome Biogenesis: Parallel Assembly Pathways for the 30S Subunit

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...

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Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 2010-10, Vol.330 (6004), p.673-677
Main Authors: Mulder, Anke M, Yoshioka, Craig, Beck, Andrea H, Bunner, Anne E, Milligan, Ronald A, Potter, Clinton S, Carragher, Bridget, Williamson, James R
Format: Article
Language:English
Subjects:
Bacterial Proteins - chemistry
Bacterial Proteins - metabolism
Biological and medical sciences
Cellular biology
Crystal structure
Deoxyribonucleic acid
DNA
E coli
Electron microscopes
Electron microscopy
Escherichia coli
Fundamental and applied biological sciences. Psychology
Head
Image Processing, Computer-Assisted
Kinetics
Mass Spectrometry
Microscopy, Electron - methods
Models, Molecular
Molecular and cellular biology
Molecular genetics
Nucleic Acid Conformation
Protein Binding
Protein Conformation
Proteins
Ribosomal proteins
Ribosomal Proteins - chemistry
Ribosomal Proteins - metabolism
Ribosome Subunits, Small, Bacterial - chemistry
Ribosome Subunits, Small, Bacterial - metabolism
Ribosome Subunits, Small, Bacterial - ultrastructure
Ribosomes
RNA
RNA, Bacterial - chemistry
RNA, Ribosomal - chemistry
Thermodynamics
Translation. Translation factors. Protein processing
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Summary: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.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.1193220