Chapter 22 : Proteins That Chaperone RNA Regulation

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Noncoding RNA sequences fold into useful structures that regulate gene expression as ribozymes, metabolite-binding sensors, or antisense RNAs ( ). These regulatory RNAs are chaperoned by diverse families of RNA-binding proteins, and the loss of RNA chaperone proteins can lead to impaired growth, reduced tolerance to stress, and reduced virulence ( ). RNA chaperones also facilitate conformational rearrangements during ribosome biogenesis ( ) and eukaryotic pre-mRNA splicing ( ).

Citation: Woodson S, Panja S, Santiago-Frangos A. 2019. Proteins That Chaperone RNA Regulation, p 385-397. In Storz G, Papenfort K (ed), Regulating with RNA in Bacteria and Archaea. ASM Press, Washington, DC. doi: 10.1128/microbiolspec.RWR-0026-2018
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Figure 1

Iterative annealing of RNA by chaperones. Typical kinetic mechanism for forming RNA secondary (2D) structure (left) and native tertiary structure (right). Assembly of the double helices (cylinders) into compact intermediates is followed by further reorganization of tertiary interactions to produce the native RNA. Because the RNA may adopt many secondary structures, some molecules fold directly to the native structure (top path) while others become trapped in nonnative structures. In the classic iterative annealing model, chaperones (gold, bottom) bind and partially unfold misfolded intermediates, then release the unfolded RNA to fold again. Adapted from reference with permission.

Citation: Woodson S, Panja S, Santiago-Frangos A. 2019. Proteins That Chaperone RNA Regulation, p 385-397. In Storz G, Papenfort K (ed), Regulating with RNA in Bacteria and Archaea. ASM Press, Washington, DC. doi: 10.1128/microbiolspec.RWR-0026-2018
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Image of Figure 2
Figure 2

Chaperone-assisted annealing of antisense RNA. Annealing of antisense or -acting sRNAs with a complementary RNA target typically begins with base-pairing between two hairpin loops (kissing complex) or a loop and a single strand (middle path). This is followed by extension of base-pairing, which often requires refolding of adjacent sequences. HIV nucleocapsid (NCp7) and Rom/Rop promote annealing by disrupting secondary structure in each RNA, lowering the energetic barriers for extending the antisense interactions (top path). NCp7 can also aggregate RNA strands to speed up initiation of base-pairing. Hfq facilitates sRNA-mRNA base-pairing by forming a ternary complex with both RNAs that increases the rate of helix nucleation (bottom path). Hfq can also favor antisense base-pairing by restructuring one or both RNAs.

Citation: Woodson S, Panja S, Santiago-Frangos A. 2019. Proteins That Chaperone RNA Regulation, p 385-397. In Storz G, Papenfort K (ed), Regulating with RNA in Bacteria and Archaea. ASM Press, Washington, DC. doi: 10.1128/microbiolspec.RWR-0026-2018
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