Protein-independent folding pathway of the 16 S rRNA 5′ domain

Tadepalli Adilakshmi, Priya Ramaswamy, Sarah A. Woodson

Research output: Contribution to journalArticle

Abstract

Evolution of the ribosome from an RNA catalyst suggests that the intrinsic folding pathway of the rRNA dictates the hierarchy of ribosome assembly. To address this possibility, we probed the tertiary folding pathway of the 5′ domain of the Escherichia coli 16 S rRNA at 20 ms intervals using X-ray-dependent hydroxyl radical footprinting. Comparison with crystallographic structures and footprinting reactions on native 30 S ribosomes showed that the RNA formed all of the predicted tertiary interactions in the absence of proteins. In 20 mM MgCl2, many tertiary interactions appeared within 20 ms. By contrast, interactions between H6, H15 and H17 near the spur of the 30 S ribosome evolved over several minutes, likely due to mispairing of a central helix junction. The kinetic folding pathway of the RNA corresponded to the expected order of protein binding, suggesting that the RNA folding pathway forms the basis for early steps of ribosome assembly.

Original languageEnglish (US)
Pages (from-to)508-519
Number of pages12
JournalJournal of Molecular Biology
Volume351
Issue number3
DOIs
StatePublished - Aug 19 2005

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Protein Folding
Ribosomes
RNA Folding
RNA
Magnesium Chloride
Protein Binding
Hydroxyl Radical
X-Rays
Escherichia coli
Proteins

Keywords

  • Hydroxyl radical footprinting
  • Ribosome assembly
  • RNA folding
  • RNA structure

ASJC Scopus subject areas

  • Virology

Cite this

Protein-independent folding pathway of the 16 S rRNA 5′ domain. / Adilakshmi, Tadepalli; Ramaswamy, Priya; Woodson, Sarah A.

In: Journal of Molecular Biology, Vol. 351, No. 3, 19.08.2005, p. 508-519.

Research output: Contribution to journalArticle

Adilakshmi, Tadepalli ; Ramaswamy, Priya ; Woodson, Sarah A. / Protein-independent folding pathway of the 16 S rRNA 5′ domain. In: Journal of Molecular Biology. 2005 ; Vol. 351, No. 3. pp. 508-519.
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