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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
12
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pubmed:dateCreated |
2010-7-5
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pubmed:abstractText |
Long-range tertiary interactions determine the three-dimensional structure of a number of metabolite-binding riboswitch RNA elements and were found to be important for their regulatory function. For the guanine-sensing riboswitch of the Bacillus subtilis xpt-pbuX operon, our previous NMR-spectroscopic studies indicated pre-formation of long-range tertiary contacts in the ligand-free state of its aptamer domain. Loss of the structural pre-organization in a mutant of this RNA (G37A/C61U) resulted in the requirement of Mg(2+) for ligand binding. Here, we investigate structural and stability aspects of the wild-type aptamer domain (Gsw) and the G37A/C61U-mutant (Gsw(loop)) of the guanine-sensing riboswitch and their Mg(2+)-induced folding characteristics to dissect the role of long-range tertiary interactions, the link between pre-formation of structural elements and ligand-binding properties and the functional stability. Destabilization of the long-range interactions as a result of the introduced mutations for Gsw(loop) or the increase in temperature for both Gsw and Gsw(loop) involves pronounced alterations of the conformational ensemble characteristics of the ligand-free state of the riboswitch. The increased flexibility of the conformational ensemble can, however, be compensated by Mg(2+). We propose that reduction of conformational dynamics in remote regions of the riboswitch aptamer domain is the minimal pre-requisite to pre-organize the core region for specific ligand binding.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/20200045-10829292,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/20200045-7679435
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Aptamers, Nucleotide,
http://linkedlifedata.com/resource/pubmed/chemical/Cations, Divalent,
http://linkedlifedata.com/resource/pubmed/chemical/Guanine,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Magnesium,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/Regulatory Sequences, Ribonucleic...
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
1362-4962
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
38
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4143-53
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pubmed:dateRevised |
2011-8-24
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pubmed:meshHeading |
pubmed-meshheading:20200045-Aptamers, Nucleotide,
pubmed-meshheading:20200045-Bacillus subtilis,
pubmed-meshheading:20200045-Cations, Divalent,
pubmed-meshheading:20200045-Guanine,
pubmed-meshheading:20200045-Ligands,
pubmed-meshheading:20200045-Magnesium,
pubmed-meshheading:20200045-Mutation,
pubmed-meshheading:20200045-Nuclear Magnetic Resonance, Biomolecular,
pubmed-meshheading:20200045-Nucleic Acid Conformation,
pubmed-meshheading:20200045-RNA, Bacterial,
pubmed-meshheading:20200045-Regulatory Sequences, Ribonucleic Acid,
pubmed-meshheading:20200045-Temperature
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pubmed:year |
2010
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pubmed:articleTitle |
Dissecting the influence of Mg2+ on 3D architecture and ligand-binding of the guanine-sensing riboswitch aptamer domain.
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pubmed:affiliation |
Institute for Organic Chemistry and Chemical Biology, Johann Wolfgang Goethe-University, Max von Laue-Strasse 7 & 9, 60438 Frankfurt am Main, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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