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Inside the 40S ribosome assembly machinery

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CURRENT OPINION IN CHEMICAL BIOLOGY
卷 15, 期 5, 页码 657-663

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CURRENT BIOLOGY LTD
DOI: 10.1016/j.cbpa.2011.07.023

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资金

  1. NIH [1R01GM086451]
  2. NSF [MCB0845156]
  3. AHA
  4. Div Of Molecular and Cellular Bioscience
  5. Direct For Biological Sciences [1062243] Funding Source: National Science Foundation

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Ribosome assembly involves rRNA transcription, modification, folding and cleavage from precursor transcripts, and association of ribosomal proteins (Rps). In bacteria, this complex process requires only a handful of proteins in addition to those needed for rRNA transcription, modification and cleavage, while in eukaryotes a large machinery comprising similar to 200 proteins in the yeast S. cerevisiae has been identified. Furthermore, while the bacterial assembly factors generally produce only cold-sensitive phenotypes upon deletion, most of the eukaryotic assembly factors are essential, comprising similar to 20% of essential yeast proteins. This review explores recent rapid progress in the structural and functional dissection of the 40S assembly machinery.

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