» Articles » PMID: 26343759

A Highly Coupled Network of Tertiary Interactions in the SAM-I Riboswitch and Their Role in Regulatory Tuning

Overview
Journal J Mol Biol
Publisher Elsevier
Date 2015 Sep 8
PMID 26343759
Citations 8
Authors
Affiliations
Soon will be listed here.
Abstract

RNA folding in vivo is significantly influenced by transcription, which is not necessarily recapitulated by Mg(2+)-induced folding of the corresponding full-length RNA in vitro. Riboswitches that regulate gene expression at the transcriptional level are an ideal system for investigating this aspect of RNA folding as ligand-dependent termination is obligatorily co-transcriptional, providing a clear readout of the folding outcome. The folding of representative members of the SAM-I family of riboswitches has been extensively analyzed using approaches focusing almost exclusively upon Mg(2+) and/or S-adenosylmethionine (SAM)-induced folding of full-length transcripts of the ligand binding domain. To relate these findings to co-transcriptional regulatory activity, we have investigated a set of structure-guided mutations of conserved tertiary architectural elements of the ligand binding domain using an in vitro single-turnover transcriptional termination assay, complemented with phylogenetic analysis and isothermal titration calorimetry data. This analysis revealed a conserved internal loop adjacent to the SAM binding site that significantly affects ligand binding and regulatory activity. Conversely, most single point mutations throughout key conserved features in peripheral tertiary architecture supporting the SAM binding pocket have relatively little impact on riboswitch activity. Instead, a secondary structural element in the peripheral subdomain appears to be the key determinant in observed differences in regulatory properties across the SAM-I family. These data reveal a highly coupled network of tertiary interactions that promote high-fidelity co-transcriptional folding of the riboswitch but are only indirectly linked to regulatory tuning.

Citing Articles

Two riboswitch classes that share a common ligand-binding fold show major differences in the ability to accommodate mutations.

Srivastava Y, Akinyemi O, Rohe T, Pritchett E, Baker C, Sharma A Nucleic Acids Res. 2024; 52(21):13152-13173.

PMID: 39413212 PMC: 11602147. DOI: 10.1093/nar/gkae886.


A riboswitch separated from its ribosome-binding site still regulates translation.

Schroeder G, Akinyemi O, Malik J, Focht C, Pritchett E, Baker C Nucleic Acids Res. 2023; 51(5):2464-2484.

PMID: 36762498 PMC: 10018353. DOI: 10.1093/nar/gkad056.


SPRINT: a Cas13a-based platform for detection of small molecules.

Iwasaki R, Batey R Nucleic Acids Res. 2020; 48(17):e101.

PMID: 32797156 PMC: 7515716. DOI: 10.1093/nar/gkaa673.


High Affinity Binding of N2-Modified Guanine Derivatives Significantly Disrupts the Ligand Binding Pocket of the Guanine Riboswitch.

Matyjasik M, Hall S, Batey R Molecules. 2020; 25(10).

PMID: 32414072 PMC: 7287874. DOI: 10.3390/molecules25102295.


Transcriptional and translational S-box riboswitches differ in ligand-binding properties.

Bhagdikar D, Grundy F, Henkin T J Biol Chem. 2020; 295(20):6849-6860.

PMID: 32209653 PMC: 7242704. DOI: 10.1074/jbc.RA120.012853.


References
1.
Daldrop P, Masquida B, Lilley D . The functional exchangeability of pk- and k-turns in RNA structure. RNA Biol. 2013; 10(3):445-52. PMC: 3672288. DOI: 10.4161/rna.23673. View

2.
Stoddard C, Montange R, Hennelly S, Rambo R, Sanbonmatsu K, Batey R . Free state conformational sampling of the SAM-I riboswitch aptamer domain. Structure. 2010; 18(7):787-97. PMC: 2917978. DOI: 10.1016/j.str.2010.04.006. View

3.
McDaniel B, Grundy F, Kurlekar V, Tomsic J, Henkin T . Identification of a mutation in the Bacillus subtilis S-adenosylmethionine synthetase gene that results in derepression of S-box gene expression. J Bacteriol. 2006; 188(10):3674-81. PMC: 1482843. DOI: 10.1128/JB.188.10.3674-3681.2006. View

4.
Waterhouse A, Procter J, Martin D, Clamp M, Barton G . Jalview Version 2--a multiple sequence alignment editor and analysis workbench. Bioinformatics. 2009; 25(9):1189-91. PMC: 2672624. DOI: 10.1093/bioinformatics/btp033. View

5.
Edwards A, Batey R . A structural basis for the recognition of 2'-deoxyguanosine by the purine riboswitch. J Mol Biol. 2008; 385(3):938-48. PMC: 2997738. DOI: 10.1016/j.jmb.2008.10.074. View