RNA-binding proteins (RBPs) are typically thought of as proteins that bind RNA through one or multiple globular RNA-binding domains (RBDs) and change the fate or function of the bound RNAs. Several hundred such RBPs have been discovered and investigated over the years. Recent proteome-wide studies have more than doubled the number of proteins implicated in RNA binding and uncovered hundreds of additional RBPs lacking conventional RBDs. In this Review, we discuss these new RBPs and the emerging understanding of their unexpected modes of RNA binding, which can be mediated by intrinsically disordered regions, protein-protein interaction interfaces and enzymatic cores, among others. We also discuss the RNA targets and molecular and cellular functions of the new RBPs, as well as the possibility that some RBPs may be regulated by RNA rather than regulate RNA.

/pdf/a-brave-new-world-of-rna-binding-proteins-1swbtoy77j.pdf

A brave new world of RNA-binding proteins

The crystal structure of the bacterial 70S ribosome refined to 2.8 angstrom resolution reveals atomic details of its interactions with messenger RNA (mRNA) and transfer RNA (tRNA). A metal ion stabilizes a kink in the mRNA that demarcates the boundary between A and P sites, which is potentially important to prevent slippage of mRNA. Metal ions also stabilize the intersubunit interface. The interactions of E-site tRNA with the 50S subunit have both similarities and differences compared to those in the archaeal ribosome. The structure also rationalizes much biochemical and genetic data on translation.

https://science.sciencemag.org/content/sci/313/5795/1935.full.pdf

Structure of the 70S Ribosome Complexed with mRNA and tRNA

Crystal structures of the 30S ribosomal subunit in complex with messenger RNA and cognate transfer RNA in the A site, both in the presence and absence of the antibiotic paromomycin, have been solved at between 3.1 and 3.3 angstroms resolution. Cognate transfer RNA (tRNA) binding induces global domain movements of the 30S subunit and changes in the conformation of the universally conserved and essential bases A1492, A1493, and G530 of 16S RNA. These bases interact intimately with the minor groove of the first two base pairs between the codon and anticodon, thus sensing Watson-Crick base-pairing geometry and discriminating against near-cognate tRNA. The third, or “wobble,” position of the codon is free to accommodate certain noncanonical base pairs. By partially inducing these structural changes, paromomycin facilitates binding of near-cognate tRNAs. During protein synthesis, the ribosome catalyzes the sequential addition of amino acids to a growing polypeptide chain, using mRNA as a template and aminoacylated tRNAs (aatRNAs) as substrates. Correct base pairing between the three bases of the codon on mRNA and those of the anticodon of the cognate aatRNA dictates the sequence of the polypeptide

https://science.sciencemag.org/content/sci/292/5518/897.full.pdf

Recognition of Cognate Transfer RNA by the 30S Ribosomal Subunit

The ability of aromatic rings to act as acceptors in hydrogen bonds has been demonstrated extensively both by experimental and by theoretical means. Countless examples of D-H...pi (H...pi, D = O, N, C) interactions have been found in the three-dimensional structures of proteins. Much less is known with regard to the occurrence of other possible noncovalent interactions with aromatics in macromolecular structures, those with a geometry that points oxygen lone pairs into the face of a pi system. There has been a growing interest in such lp...pi interactions in recent years, but the binding energies have mostly been studied using small-molecule model systems. We have conducted a survey of lp...pi interactions in crystal structures of DNA, RNA, and proteins and used ab initio calculations to estimate their energies. Our results demonstrate that such interactions are more common in nucleic acids and that significant binding energies only result when the aromatic system is positively polarized, for example, due to protonation of a nucleobase.

Lone pair-aromatic interactions: to stabilize or not to stabilize.

The problem of how ions influence the folding of RNA into specific tertiary structures is being addressed from both thermodynamic (by how much do different salts affect the free energy change of folding) and structural (how are ions arranged on or near an RNA and what kinds of environments do they occupy) points of view. The challenge is to link these different approaches in a theoretical framework that relates the energetics of ion-RNA interactions to the spatial distribution of ions. This review distinguishes three different kinds of ion environments that differ in the extent of direct ion-RNA contacts and the degree to which the ion hydration is perturbed, and summarizes the current understanding of the way each environment relates to the overall energetics of RNA folding.

Ions and RNA Folding

The crystal structure of the monoclinic form of yeast phenylalanine tRNA has been redetermined at a resolution of 1.93 A. The structure of yeast tRNAphe described here is more accurate than its predecessors not only because it incorporates higher resolution data, but also because it has been refined using techniques that had not been developed when its predecessors were determined more than 20 years ago. The 1.93 A resolution version of this structure differs interestingly from its predecessors in its details. In loop regions particularly, the backbone torsion angles in the new structure are not the same as those reported earlier. Several new divalent cation binding sites have been identified, and the water structure that has emerged is also different.

The crystal structure of yeast phenylalanine tRNA at 1.93 A resolution: a classic structure revisited.

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The crystal structure of yeast phenylalanine tRNA at 1.93 A resolution: a classic structure revisited.