Faculty Opinions recommendation of The UAA/GAN internal loop motif: a new RNA structural element that forms a cross-strand AAA stack and long-range tertiary interactions.

Author(s):  
Scott Silverman
Author(s):  
Christian Richter ◽  
Katharina F. Hohmann ◽  
Sabrina Toews ◽  
Daniel Mathieu ◽  
Nadide Altincekic ◽  
...  

AbstractThe stem-loop (SL1) is the 5'-terminal structural element within the single-stranded SARS-CoV-2 RNA genome. It is formed by nucleotides 7–33 and consists of two short helical segments interrupted by an asymmetric internal loop. This architecture is conserved among Betacoronaviruses. SL1 is present in genomic SARS-CoV-2 RNA as well as in all subgenomic mRNA species produced by the virus during replication, thus representing a ubiquitous cis-regulatory RNA with potential functions at all stages of the viral life cycle. We present here the 1H, 13C and 15N chemical shift assignment of the 29 nucleotides-RNA construct 5_SL1, which denotes the native 27mer SL1 stabilized by an additional terminal G-C base-pair.


1982 ◽  
Vol 205 (2) ◽  
pp. 457-460 ◽  
Author(s):  
R Malathi ◽  
N Yathindra

A distance plot obtained using the blocked nucleotide concept, which regards the repeating nucleotide moieties to be made up of two blocks of nearly equal magnitude, has permitted us to visualize the polynucleotide backbone folding in yeast tRNAPhe. The plot clearly manifests medium- and long-range tertiary interactions involving various structural domains. Apart from the well known T psi-D loop interactions, other long-range interactions associated with the variable loop as well as the D loop are explicitly seen. Most importantly, the plot reveals an approximate two-fold symmetry in the molecule between the domains related to the tertiary interactions in addition to the symmetry between long helical domains. The different patterns on the plot are interpreted in terms of helix-helix, loop-helix and loop-loop interactions.


2015 ◽  
Author(s):  
Van K Duesterberg ◽  
Irena T Fischer-Hwang ◽  
Christian F Perez ◽  
Daniel W Hogan ◽  
Steven M Block

2014 ◽  
Vol 136 (18) ◽  
pp. 6643-6648 ◽  
Author(s):  
Xuesong Shi ◽  
Namita Bisaria ◽  
Tara L. Benz-Moy ◽  
Steve Bonilla ◽  
Dmitri S. Pavlichin ◽  
...  

2005 ◽  
Vol 102 (5) ◽  
pp. 1430-1435 ◽  
Author(s):  
C. W. Bertoncini ◽  
Y.-S. Jung ◽  
C. O. Fernandez ◽  
W. Hoyer ◽  
C. Griesinger ◽  
...  

2020 ◽  
Author(s):  
Jeffrey E. Ehrhardt ◽  
Kevin M. Weeks

AbstractMethods for capturing the folding dynamics of functionally important RNAs, especially large RNAs, have relied primarily on global measurements of structure or on per-nucleotide chemical probing. These approaches infer, but do not directly measure, through-space tertiary interactions. Here we introduce trimethyloxonium (TMO) as a chemical probe for RNA. TMO enables time-resolved, single-molecule, through-space structure probing of RNA folding using a correlated chemical probing framework. TMO methylates RNA about 90 times faster than the widely used dimethyl sulfate probe, allowing structure interrogation on the second time scale. We used TMO to monitor folding of the RNase P RNA – a functional RNA with extensive long-range and noncanonical interactions – by direct measurement of through-space tertiary interactions in a time-resolved way. Time-dependent correlation changes directly revealed the central role of a long-range tertiary loop-loop interaction that guides native RNA folding. Single-molecule, time-resolved RNA structure probing with TMO is poised to reveal a wide range of dynamic RNA folding processes and principles of RNA folding.


eLife ◽  
2015 ◽  
Vol 4 ◽  
Author(s):  
Van K Duesterberg ◽  
Irena T Fischer-Hwang ◽  
Christian F Perez ◽  
Daniel W Hogan ◽  
Steven M Block

The thiamine pyrophosphate (TPP) riboswitch is a cis-regulatory element in mRNA that modifies gene expression in response to TPP concentration. Its specificity is dependent upon conformational changes that take place within its aptamer domain. Here, the role of tertiary interactions in ligand binding was studied at the single-molecule level by combined force spectroscopy and Förster resonance energy transfer (smFRET), using an optical trap equipped for simultaneous smFRET. The ‘Force-FRET’ approach directly probes secondary and tertiary structural changes during folding, including events associated with binding. Concurrent transitions observed in smFRET signals and RNA extension revealed differences in helix-arm orientation between two previously-identified ligand-binding states that had been undetectable by spectroscopy alone. Our results show that the weaker binding state is able to bind to TPP, but is unable to form a tertiary docking interaction that completes the binding process. Long-range tertiary interactions stabilize global riboswitch structure and confer increased ligand specificity.


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