ArticleBiochemical and biophysical research communications2008
Characterizing riboswitch function: identification of Mg2+ binding site in T box antiterminator RNA.
Article in Biochemical and biophysical research communications, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 10 citations in OpenAlex.
- Identification of Spermidine Binding Site in T-box Riboswitch Antiterminator RNA.Chemical biology & drug design · 2016Article
- Factors that influence T box riboswitch efficacy and tRNA affinity.Bioorganic & medicinal chemistry · 2015Article
- Interfacing medicinal chemistry with structural bioinformatics: implications for T box riboswitch RNA drug discovery.BMC bioinformatics · 2012Article
- Ligand-induced changes in T box antiterminator RNA stability.Chemical biology & drug design · 2012Article
- Modulation of the stability of the Salmonella fourU-type RNA thermometer.Nucleic acids research · 2011Article
- Fluorescence probing of T box antiterminator RNA: insights into riboswitch discernment of the tRNA discriminator base.Biochemical and biophysical research communications · 2009Article
- T box transcription antitermination riboswitch: influence of nucleotide sequence and orientation on tRNA binding by the antiterminator element.Biochimica et biophysica acta · 2009Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
T box bacterial genes utilize a riboswitch mechanism to regulate gene expression at the transcriptional level. Complementary base pairing of the 5'-untranslated mRNA with uncharged cognate tRNA stabilizes formation of an antiterminator element and permits complete transcription. In the absence of tRNA, a mutually exclusive RNA terminator element forms and results in transcription termination. This regulatory mechanism requires divalent metal ions at the antitermination event. The structural effects of Mg(2+) binding to antiterminator model RNA were investigated to ascertain if this requirement is due to the presence of a specific metal ion binding site in the antiterminator. Spectroscopic analysis identified the presence of a hydrated, diffuse Mg(2+) binding site. The results indicate that the mechanistic requirement for divalent metal ions is not due to Mg(2+)-induced pre-formation of a functional antiterminator receptor; rather, Mg(2+) binds in a helical region of high phylogenetic sequence conservation adjacent to the tRNA binding site.
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