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The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
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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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RNA viruses are categorized into positive-strand, negative-strand, or double-stranded groups based on their genomic structure and replication mechanisms. This classification dictates how they exploit host cellular machinery for protein synthesis and replication. Some RNA viruses also utilize reverse transcription as part of their life cycle, further diversifying their replication strategies.Positive-Strand RNA VirusesPositive-strand RNA viruses have genomes that function directly as messenger...
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RNA chaperones encoded by RNA viruses.

Jie Yang1, Hongjie Xia1, Qi Qian1

  • 1State Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan, 430072, China.

Virologica Sinica
|December 31, 2015
PubMed
Summary

Viral RNA chaperones are crucial for RNA folding and viral life cycles. This review highlights their activities and functions, often overlooked compared to RNA helicases.

Keywords:
ATP-independent helix-destabilizing activityRNA chaperoneRNA viruseskinetic trapviral life cycle

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Area of Science:

  • Molecular Biology
  • Virology
  • Biochemistry

Background:

  • Ribonucleic acids (RNAs) require precise tertiary structures for function.
  • RNA folding is inherently slow and challenging due to high structural flexibility.
  • Cells and viruses utilize RNA remodeling proteins like helicases and chaperones to facilitate proper RNA structure.

Purpose of the Study:

  • To review the activities and functions of RNA chaperones encoded by RNA viruses.
  • To highlight recently identified and characterized viral RNA chaperones.
  • To provide an overview of these essential viral proteins and their roles in viral life cycles.

Main Methods:

  • Literature review of existing research on viral RNA chaperones.
  • Analysis of characterized RNA chaperone activities.
  • Synthesis of information on the functions of these proteins in viral processes.

Main Results:

  • RNA chaperones, particularly virus-encoded ones, play pivotal roles in viral RNA processing.
  • These proteins are essential for various stages of the viral life cycle.
  • Recent years have seen increased identification and characterization of these important viral factors.

Conclusions:

  • Virus-encoded RNA chaperones are critical, yet often understudied, components of viral replication.
  • Understanding their mechanisms is key to comprehending viral pathogenesis.
  • Further research into RNA chaperones offers potential therapeutic targets.