Difference between revisions of "Team:RHIT"

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<p> Our project focuses on controlling the expression of a mitochondrial ribosomal protein gene (<i>MRPS12</i>). By creating a genetic switch that can repress or derepress <i>MRPS12</i>, we can affect whether yeast (<i>S. cerevisiae</i>) undergoes aerobic respiration or fermentation. MRPS12 is vital to mitochondrial ribosomal function, therefore when it is not expressed, the mitochondrial ribosomes cannot translate the proteins required for the electron transport chain. Following this line of progression, when <i>MRPS12</i> is repressed, aerobic respiration does not occur and the cells are forced to ferment. </p>  
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<p> Our project focuses on controlling aerobic respiration in the yeast <i>Saccharomyces cerevisiae</i>. We will address this objective by regulating the expression of mitochondrial ribosomal protein MRPS12. This protein is essential to the function of mitochondrial ribosomes, which produce key components of the electron transport chain. Without these components, the electron transport chain is disabled and aerobic respiration is not possible. </p>  
  
 
<img style="width:50%" src="https://static.igem.org/mediawiki/2015/5/57/RHIT_HOMEPAGE.png">
 
<img style="width:50%" src="https://static.igem.org/mediawiki/2015/5/57/RHIT_HOMEPAGE.png">

Revision as of 01:21, 18 September 2015

Welcome to Rose-Hulman's MitochONdriOFF project!

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Our project focuses on controlling aerobic respiration in the yeast Saccharomyces cerevisiae. We will address this objective by regulating the expression of mitochondrial ribosomal protein MRPS12. This protein is essential to the function of mitochondrial ribosomes, which produce key components of the electron transport chain. Without these components, the electron transport chain is disabled and aerobic respiration is not possible.

Our project used yeast strains that had their endogenous MRPS12 gene disrupted with a kanamycin gene. We showed that when the MRPS12 gene was reintroduced to this strain on a plasmid, ETC function was restored.

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