Sandra Vergara | University of Massachusetts Medical School (original) (raw)

Sandra Vergara

Supervisors: Craig Mello

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Papers by Sandra Vergara

Research paper thumbnail of Negative feedback regulation of the yeast CTH1 and CTH2 mRNA binding proteins is required for adaptation to iron deficiency and iron supplementation.

Research paper thumbnail of Ironing Out a Midlife Crisis

Research paper thumbnail of Post-Transcriptional Regulation of Gene Expression In Response to Iron Deficiency In Saccharomyces Cerevisiae

Research paper thumbnail of The Cth2 ARE-Binding Protein Recruits the Dhh1 Helicase to Promote the Decay of Succinate Dehydrogenase SDH4 MRNA In Response to Iron Deficiency

Journal of Biological …, Jan 1, 2008

Iron is an essential nutrient that participates as a redox co-factor in a broad range of cellular... more Iron is an essential nutrient that participates as a redox co-factor in a broad range of cellular processes. In response to iron deficiency, the budding yeast Saccharomyces cerevisiae induces the expression of the Cth1 and Cth2 mRNA-binding proteins to promote a genome-wide remodeling of cellular metabolism that contributes to the optimal utilization of iron. Cth1 and Cth2 proteins bind to specific AU-rich elements within the 3'-untranslated region of many mRNAs encoding proteins involved in iron-dependent pathways, thereby promoting their degradation. Here, we show that the DEAD box Dhh1 helicase plays a crucial role in the mechanism of Cth2-mediated mRNA turnover. Yeast two-hybrid experiments indicate that Cth2 protein interacts in vivo with the carboxyl-terminal domain of Dhh1. We demonstrate that the degradation of succinate dehydrogenase SDH4 mRNA, a known target of Cth2 on iron-deficient conditions, depends on Dhh1. In addition, we localize the Cth2 protein to cytoplasmic processing bodies in strains defective in the 5' to 3' mRNA decay pathway. Finally, the degradation of trapped SDH4 mRNA intermediates by Cth2 supports the 5' to 3' directionality of mRNA turnover. Taken together, these results suggest that Cth2 protein recruits the Dhh1 helicase to ARE-containing mRNAs to promote mRNA decay.

Research paper thumbnail of Post-Transcriptional Regulation of Gene Expression In Response to Iron Deficiency In

Research paper thumbnail of Cooperation of Two MRNA-Binding Proteins Drives Metabolic Adaptation to Iron Deficiency

Cell metabolism, Jan 1, 2008

Research paper thumbnail of Biochemical and Functional Characterization of the Actin-Binding Activity of the B Subunit of Yeast Vacuolar H+-ATPase

Journal of Experimental …, Jan 1, 2008

Research paper thumbnail of The Amino-Terminal Domain of the E Subunit of Vacuolar H+-ATPase (V-ATPase) Interacts With the H Subunit and is Required for V-ATPase Function

Journal of Biological …, Jan 1, 2002

Research paper thumbnail of Actin Binding Activity of Subunit B of Vacuolar H+-ATPase is Involved In Its Targeting to Ruffled Membranes of Osteoclasts

Journal of Bone …, Jan 1, 2006

Research paper thumbnail of Early Recruitment of AU-Rich Element-Containing MRNAs Determines Their Cytosolic Fate During Iron Deficiency

Molecular and Cellular Biology, Jan 1, 2011

Research paper thumbnail of Negative feedback regulation of the yeast CTH1 and CTH2 mRNA binding proteins is required for adaptation to iron deficiency and iron supplementation.

Research paper thumbnail of Ironing Out a Midlife Crisis

Research paper thumbnail of Post-Transcriptional Regulation of Gene Expression In Response to Iron Deficiency In Saccharomyces Cerevisiae

Research paper thumbnail of The Cth2 ARE-Binding Protein Recruits the Dhh1 Helicase to Promote the Decay of Succinate Dehydrogenase SDH4 MRNA In Response to Iron Deficiency

Journal of Biological …, Jan 1, 2008

Iron is an essential nutrient that participates as a redox co-factor in a broad range of cellular... more Iron is an essential nutrient that participates as a redox co-factor in a broad range of cellular processes. In response to iron deficiency, the budding yeast Saccharomyces cerevisiae induces the expression of the Cth1 and Cth2 mRNA-binding proteins to promote a genome-wide remodeling of cellular metabolism that contributes to the optimal utilization of iron. Cth1 and Cth2 proteins bind to specific AU-rich elements within the 3'-untranslated region of many mRNAs encoding proteins involved in iron-dependent pathways, thereby promoting their degradation. Here, we show that the DEAD box Dhh1 helicase plays a crucial role in the mechanism of Cth2-mediated mRNA turnover. Yeast two-hybrid experiments indicate that Cth2 protein interacts in vivo with the carboxyl-terminal domain of Dhh1. We demonstrate that the degradation of succinate dehydrogenase SDH4 mRNA, a known target of Cth2 on iron-deficient conditions, depends on Dhh1. In addition, we localize the Cth2 protein to cytoplasmic processing bodies in strains defective in the 5' to 3' mRNA decay pathway. Finally, the degradation of trapped SDH4 mRNA intermediates by Cth2 supports the 5' to 3' directionality of mRNA turnover. Taken together, these results suggest that Cth2 protein recruits the Dhh1 helicase to ARE-containing mRNAs to promote mRNA decay.

Research paper thumbnail of Post-Transcriptional Regulation of Gene Expression In Response to Iron Deficiency In

Research paper thumbnail of Cooperation of Two MRNA-Binding Proteins Drives Metabolic Adaptation to Iron Deficiency

Cell metabolism, Jan 1, 2008

Research paper thumbnail of Biochemical and Functional Characterization of the Actin-Binding Activity of the B Subunit of Yeast Vacuolar H+-ATPase

Journal of Experimental …, Jan 1, 2008

Research paper thumbnail of The Amino-Terminal Domain of the E Subunit of Vacuolar H+-ATPase (V-ATPase) Interacts With the H Subunit and is Required for V-ATPase Function

Journal of Biological …, Jan 1, 2002

Research paper thumbnail of Actin Binding Activity of Subunit B of Vacuolar H+-ATPase is Involved In Its Targeting to Ruffled Membranes of Osteoclasts

Journal of Bone …, Jan 1, 2006

Research paper thumbnail of Early Recruitment of AU-Rich Element-Containing MRNAs Determines Their Cytosolic Fate During Iron Deficiency

Molecular and Cellular Biology, Jan 1, 2011

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