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Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...
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An In Vitro Assay to Detect tRNA-Isopentenyl Transferase Activity
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RNA modification enzyme TruB is a tRNA chaperone.

Laura Carole Keffer-Wilkes1, Govardhan Reddy Veerareddygari1, Ute Kothe2

  • 1Alberta RNA Research and Training Institute, Department of Chemistry and Biochemistry, University of Lethbridge, Lethbridge, AB, Canada T1K 3M4.

Proceedings of the National Academy of Sciences of the United States of America
|November 17, 2016
PubMed
Summary

Bacterial tRNA pseudouridine synthase TruB acts as an RNA chaperone, folding transfer RNAs (tRNAs) independently of its catalytic function. This chaperone activity is crucial for bacterial fitness and cellular function.

Keywords:
RNA chaperoneRNA foldingRNA modificationpseudouridinetRNA

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Area of Science:

  • Molecular Biology
  • Biochemistry
  • Genetics

Background:

  • Cellular RNAs undergo chemical modifications by numerous enzymes, but their functional significance is often unknown.
  • Pseudouridine formation in the tRNA TΨC arm by bacterial tRNA pseudouridine synthase TruB is one such modification with unclear function.

Purpose of the Study:

  • To investigate if RNA modification enzymes, using TruB as a model, also function as RNA chaperones.
  • To elucidate the molecular mechanism and biological importance of TruB's potential RNA chaperone activity.

Main Methods:

  • Utilizing TruB as a model enzyme to study tRNA folding.
  • Employing rapid kinetic stopped-flow analysis to determine the mechanism of TruB's interaction with tRNA.
  • Assessing the fitness of Escherichia coli strains expressing different TruB variants.

Main Results:

  • TruB demonstrates tRNA folding activity independent of its catalytic pseudouridine formation.
  • TruB binds and unfolds both misfolded and correctly folded tRNAs, offering misfolded tRNAs a chance to refold.
  • Escherichia coli strains expressing TruB variants deficient in tRNA binding and folding exhibit reduced competitiveness compared to wild-type strains.

Conclusions:

  • The pseudouridine synthase TruB possesses significant tRNA chaperone activity, essential for bacterial fitness.
  • The molecular mechanism involves binding and unfolding of tRNAs to facilitate proper folding.
  • This finding suggests that other RNA modification enzymes may also possess chaperone functions.