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TitleFunctional domains of the 50S subunit mature late in the assembly process.
Journal, issue, pagesNucleic Acids Res, Vol. 42, Issue 5, Page 3419-3435, Year 2014
Publish dateDec 13, 2013
AuthorsAhmad Jomaa / Nikhil Jain / Joseph H Davis / James R Williamson / Robert A Britton / Joaquin Ortega /
PubMed AbstractDespite the identification of many factors that facilitate ribosome assembly, the molecular mechanisms by which they drive ribosome biogenesis are poorly understood. Here, we analyze the late stages ...Despite the identification of many factors that facilitate ribosome assembly, the molecular mechanisms by which they drive ribosome biogenesis are poorly understood. Here, we analyze the late stages of assembly of the 50S subunit using Bacillus subtilis cells depleted of RbgA, a highly conserved GTPase. We found that RbgA-depleted cells accumulate late assembly intermediates bearing sub-stoichiometric quantities of ribosomal proteins L16, L27, L28, L33a, L35 and L36. Using a novel pulse labeling/quantitative mass spectrometry technique, we show that this particle is physiologically relevant and is capable of maturing into a complete 50S particle. Cryo-electron microscopy and chemical probing revealed that the central protuberance, the GTPase associating region and tRNA-binding sites in this intermediate are unstructured. These findings demonstrate that key functional sites of the 50S subunit remain unstructured until late stages of maturation, preventing the incomplete subunit from prematurely engaging in translation. Finally, structural and biochemical analysis of a ribosome particle depleted of L16 indicate that L16 binding is necessary for the stimulation of RbgA GTPase activity and, in turn, release of this co-factor, and for conversion of the intermediate to a complete 50S subunit.
External linksNucleic Acids Res / PubMed:24335279 / PubMed Central
MethodsEM (single particle)
Resolution11.0 - 13.0 Å
Structure data

EMDB-5787:
Cryo-electron microscopy of the 50S ribosomal subunit from Bacillus subtilis
Method: EM (single particle) / Resolution: 11.0 Å

EMDB-5788:
Cryo-electron microscopy of the 50S ribosomal subunit from Bacillus subtilis without L16 ribosomal protein
Method: EM (single particle) / Resolution: 13.0 Å

EMDB-5789:
Cryo-electron microscopy of an immature 50S ribosomal subunit (45S particle) from Bacillus depleted of RbgA (YlqF), conformation 1
Method: EM (single particle) / Resolution: 13.0 Å

EMDB-5790:
Cryo-electron microscopy of an immature 50S ribosomal subunit (45S particle) from Bacillus subtilis depleted of RbgA (YlqF), conformation 2
Method: EM (single particle) / Resolution: 13.0 Å

EMDB-5791:
Cryo-electron microscopy of an immature 50S ribosomal subunit (45S particle) from Bacillus subtilis depleted of RbgA (YlqF), conformation 3
Method: EM (single particle) / Resolution: 13.0 Å

EMDB-5792:
Cryo-electron microscopy of an immature 50S ribosomal subunit (45S particle) from Bacillus subtilis depleted of RbgA (YlqF), conformation 4
Method: EM (single particle) / Resolution: 13.0 Å

Source
  • Bacillus subtilis (bacteria)

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