Switching the light on plant riboswitches.
ABSTRACT Riboswitches are natural RNA sensors that affect post-transcriptional processes via their capacity to bind small molecules. To date, these mRNA structures have been shown to regulate the biosynthesis of essential metabolites, including vitamins and amino acids. Although bacterial riboswitches are widespread and characterized, only a single eukaryotic, thiamin-pyrophosphate-binding riboswitch has recently been discovered to direct gene expression by regulating mRNA splicing in fungi, green algae and land plants. It is unclear how widespread riboswitches are and what additional roles they have in eukaryotes. When engineered in plants, riboswitches can function autonomously to modulate gene expression. These discoveries not only trigger novel findings regarding RNA switches in plants, but also spur the exploitation of riboswitches for monitoring metabolite concentrations in planta.
Full-textDOI: · Available from: Samuel Bocobza, Jun 16, 2014
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ABSTRACT: Ascorbate (vitamin C) is an essential antioxidant and enzyme cofactor in both plants and animals. Ascorbate concentration is tightly regulated in plants, partly to respond to stress. Here, we demonstrate that ascorbate concentrations are determined via the posttranscriptional repression of GDP-l-galactose phosphorylase (GGP), a major control enzyme in the ascorbate biosynthesis pathway. This regulation requires a cis-acting upstream open reading frame (uORF) that represses the translation of the downstream GGP open reading frame under high ascorbate concentration. Disruption of this uORF stops the ascorbate feedback regulation of translation and results in increased ascorbate concentrations in leaves. The uORF is predicted to initiate at a noncanonical codon (ACG rather than AUG) and encode a 60- to 65-residue peptide. Analysis of ribosome protection data from Arabidopsis thaliana showed colocation of high levels of ribosomes with both the uORF and the main coding sequence of GGP. Together, our data indicate that the noncanonical uORF is translated and encodes a peptide that functions in the ascorbate inhibition of translation. This posttranslational regulation of ascorbate is likely an ancient mechanism of control as the uORF is conserved in GGP genes from mosses to angiosperms. © 2015 American Society of Plant Biologists. All rights reserved.The Plant Cell 02/2015; 27(3). DOI:10.1105/tpc.114.133777
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ABSTRACT: Abstract Metabolites regulate their own production by directly interacting with highly conserved regions of mRNA that are capable of forming discrete tertiary structures. Such regions of mRNA are called riboswitches. The thiamine pyrophosphate (TPP) riboswitch is the most common riboswitch in different organisms. The TPP is an essential coenzyme that is synthesized by the coupling of pyrimidine (hydroxymethyl pyrimidine) and thiazole (hydroxyethyl thiazole). The TPP riboswitch was searched across all possible phyla of plant kingdom by using Arabidopsis thaliana, a model organism in which TPP riboswitch is already found. The aptameric domain of the TPP riboswitch is conserved at the sequence as well as structure levels in all chosen plant species. The sequence of the noncoding RNA that acts as a riboswitch and is folded into an appropriate stem-loop hairpin secondary structure with minimum free energy is predicted by several computational tools. Most of the secondary structures are similar but not the same, because of variation in sequence size. The TPP ligand can bind to the 3' untranslated region of the aptameric sequence, between the loops P2, P4, and P5 and the region between J2/3 and J4/5. The sequence of these loop regions in all predicted tertiary structure of the riboswitch in representative plant species-green algae to flowering plants-is the same, and the residues situated in these junctions are directly involved in binding thymine pyrophosphate and are conserved in all the representative species.Journal of computational biology: a journal of computational molecular cell biology 09/2014; 22(1). DOI:10.1089/cmb.2014.0169
IOSR Journal of Dental and Medical Sciences 01/2014; 13(6):44-47. DOI:10.9790/0853-13634447