Crystal structure of an RNA bacteriophage coat protein–operator complex

@article{Valegrd1994CrystalSO,
  title={Crystal structure of an RNA bacteriophage coat protein–operator complex},
  author={Karin Valeg{\aa}rd and James B. Murray and Peter G. Stockley and Nicola J. Stonehouse and Lars Liljas},
  journal={Nature},
  year={1994},
  volume={371},
  pages={623-626}
}
THE RNA bacteriophage MS2 is a convenient model system for the study of protein–RNA interactions. The MS2 coat protein achieves control of two distinct processes—sequence-specific RNA encapsidation and repression of replicase translation—by binding to an RNA stem–loop structure of 19 nucleotides containing the initiation codon of the replicase gene. The binding of a coat protein dimer to this hairpin shuts off synthesis of the viral replicase1, switching the viral replication cycle to virion… 

Crystal structure of the bacteriophage Qβ coat protein in complex with the RNA operator of the replicase gene.

The three-dimensional structures of two complexes between recombinant MS2 capsids and RNA operator fragments reveal sequence-specific protein-RNA interactions.

TLDR
Crystal structures of two complexes between recombinant MS2 capsids and RNA operator fragments have been determined at 2.7 A resolution using chemically synthesized variants of the stem-loop fragment and soaked them into crystals of recombinant capsids.

Protein-RNA Interactions in the Single-Stranded RNA Bacteriophages.

TLDR
In this chapter, the different ssRNA phage protein-RNA interactions, as well as some of their practical applications, are discussed in detail.

PRR1 coat protein binding to its RNA translational operator.

TLDR
The structure of virus-like particles of the small RNA phage PRR1 bound to an RNA segment corresponding to this stem-loop has been solved and the binding was compared with the related, and better investigated, phage MS2.

Role of the coat Protein-RNA interaction in the life cycle of bacteriophage MS2

  • D. Peabody
  • Biology
    Molecular and General Genetics MGG
  • 1997
TLDR
The strength of the interaction was perturbed by constructing a recombinant genome containing a super-repressing coat mutation, which reduced coat protein synthesis to a few percent of the wild-type level.

RNA recognition site of PP7 coat protein.

TLDR
The RNA structural requirements for binding to the coat protein of bacteriophage PP7, an RNA phage of Pseudomonas is described and it is found that tight binding to PP7 coat protein is favored by the existence of an 8 bp hairpin with a bulged purine on its 5' side separated by 4 bp from a 6 nt loop having the sequence Pu-U-A-G/U-G-Pu.

Crystallographic studies of RNA hairpins in complexes with recombinant MS2 capsids: implications for binding requirements.

The coat protein of bacteriophage MS2 is known to bind specifically to an RNA hairpin formed within the MS2 genome. Structurally this hairpin is built up by an RNA double helix interrupted by one
...

References

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TLDR
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Specific interaction between RNA phage coat proteins and RNA.

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TLDR
The model was successfully tested by demonstrating that oligomers with sequences quite different from the replicase initiator were able to bind coat protein, suggesting that while the hairpin loop structure is essential for protein binding, the base-paired residues do not contact the protein directly.

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TLDR
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TLDR
Analysis of synthetic oligoribonucleotides used to probe the interaction of MS2 coat protein with the translational operator of the MS2 replicase gene shows that the complex with the 5-BrU operator is more stable than the -5C variant; a result which is consistent with the formation of a Michael adduct at the - 5 position.