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<big>'''Paper of the month: May 2015'''</big>  
 
<big>'''Paper of the month: May 2015'''</big>  
* In ''B. subtilis'', ribosomal stalling is used to regulate the expression of the membrane protein biogenesis factor [[YidC2]]. This is achieved by stalling during [[translation]] of the [[MifM]] leader peptide. In the absence of structures of Gram-positive bacterial ribosomes, a molecular basis for species-specific stalling has remained unclear. [http://www.ncbi.nlm.nih.gov/pubmed/25903689 Sohmen et al.] have determined the structure of the [[MifM]]-stalled 70S [[ribosome]] and have unraveled a network of interactions between [[MifM]] and the ribosomal tunnel, which induces translational arrest. Complementary genetic analyses identify a single amino acid within [[ribosomal protein]] [[rplV|L22]] that dictates the species specificity of the stalling event.  
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* The precise quantification of the dynamic changes in metabolite concentrations is a major challenge in metabolomics. Two new studies make use of the combination of metablite-sensitive riboswitches with an ''in vitro'' selected Spinach aptamer, which binds a pro-fluorescent, cell-permeable small molecule mimic of the GFP chromophore. Fluorescence can then be determined as a measure of the concentration of the metabolite that binds the riboswitch. The present studies use this approach for the essential second messenger c-di-AMP as well as for S-adenosyl-methionine and guanine.
** '''Relevant ''Subti''Wiki pages:''' [[translation]], [[ribosome]], ''[[yidC2]]'', [[MifM]], [[rplV|L22]]
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** '''Relevant ''Subti''Wiki pages:''' [[riboswitch]], [[metabolism]], [[methods]]
<pubmed> 25903689</pubmed>
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<pubmed25964329 25965978</pubmed>
 
* [[Previous papers of the month]]
 
* [[Previous papers of the month]]
  

Revision as of 08:49, 4 June 2015

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Paper of the month: May 2015

  • The precise quantification of the dynamic changes in metabolite concentrations is a major challenge in metabolomics. Two new studies make use of the combination of metablite-sensitive riboswitches with an in vitro selected Spinach aptamer, which binds a pro-fluorescent, cell-permeable small molecule mimic of the GFP chromophore. Fluorescence can then be determined as a measure of the concentration of the metabolite that binds the riboswitch. The present studies use this approach for the essential second messenger c-di-AMP as well as for S-adenosyl-methionine and guanine.

<pubmed25964329 25965978</pubmed>


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