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Mechanisms Of Condition-Specific Regulation Of Mrna Stability By Puf Proteins: From Yeast To Humans, Joseph Russo
Mechanisms Of Condition-Specific Regulation Of Mrna Stability By Puf Proteins: From Yeast To Humans, Joseph Russo
Dissertations
RNA binding proteins regulate mRNA decay and translation, two key steps in the control of gene expression in cells. Controlling mRNA metabolism allows cells to respond rapidly to altering conditions by utilizing already available mRNA, bypassing the wait for newly transcribed mRNA. The Puf family of RNA binding proteins bind specific mRNAs through interactions with sequences located in the 3’ untranslated region (UTR). Puf proteins are conserved throughout eukaryotes and have diverse roles including stem cell maintenance, neuronal development, stress response and organelle biogenesis. In Saccharomyces cerevisiae, Puf proteins are conditionally regulated in response to the cells metabolic. Specifically, in …
Analysis Of The Condition-Specific Regulation Of Puf3p Activity And Puf3p-Mediated Translational Repression Of Mrna In Saccharomyces Cerevisiae, Melanie A. Miller
Analysis Of The Condition-Specific Regulation Of Puf3p Activity And Puf3p-Mediated Translational Repression Of Mrna In Saccharomyces Cerevisiae, Melanie A. Miller
Dissertations
The Puf family of proteins regulates aspects of eukaryotic development such as embryonic development, and memory formation by promoting translational repression and/or degradation of targeted mRNAs in the cytoplasm. Yeast Puf3p regulates mitochondria biogenesis and function by modulating the stabilities of nuclear-transcribed mitochondrial mRNAs in response to different carbon sources. Dextrose simulates rapid Puf3p-mediated degradation of its mRNA targets via decay complex recruitment. Ethanol, galactose, or raffinose promotes stabilization of mRNA targets, as Puf3p-mediated decay activity is severely inhibited or abolished. In this work, I have established that carbon source-induced inhibition of Puf3p activity is not due to decreased transcription …