Poster Title

Exploration of the Molybdenum Cofactor gene in the fruit fly Drosophila melangoster

Co-Author(s)

David Burgdorf, Olivia Thompson

Research Mentor(s)

Sandra Schulze

Affiliated Department

Biology

Sort Order

31

Start Date

18-5-2017 9:00 AM

End Date

18-5-2017 12:00 PM

Document Type

Event

Abstract

Molybdenum (Mo) is an essential trace metal found in most foods. Enzymes that require Mo cannot use this metal unless it is chelated with an organic complex called the Mo cofactor. MOCS1 is a gene that encodes an enzyme that catalyzes the first step in the synthesis of the Mo Cofactor (“MoCo”). The MOCS1 gene is extremely highly conserved, found in bacteria, fungi, plants and animals. Mutations in MOCS1 cause a disease in humans known as Molybdenum cofactor (MoCo) deficiency, which ultimately results in a combined deficiency of three essential enzymatic functions that depend on Mo: sulfite oxidase, xanthine dehydrogenase and aldehyde oxidase. These enzymes confer a protective function on the cell, by removing toxic catabolites. Sulfite oxidase, for example, is located in the mitochondrial intermembrane space, where it catalyzes the oxidation of sulfite to sulfate, removing the reactive and potentially toxic sulfite from the cell. MoCo deficiency segregates as an autosomal recessive disorder, and generally leads to early childhood death. We hypothesize that an increase in MOCS1 gene expression may have protective effects, by permitting the enzymes that depend on Mo and its cofactor to function more efficiently. Life extending strategies in model organisms have been successful when targeting similar protective pathways that also involve mitochondrial function. The work presented here outlines the preparatory phase of a longevity experiment, in which we plan to upregulate MOCS1 gene expression in fruit flies, and measure the effect on lifespan.

Rights

Copying of this document in whole or in part is allowable only for scholarly purposes. It is understood, however, that any copying or publication of this documentation for commercial purposes, or for financial gain, shall not be allowed without the author's written permission.

Language

English

Format

application/pdf

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May 18th, 9:00 AM May 18th, 12:00 PM

Exploration of the Molybdenum Cofactor gene in the fruit fly Drosophila melangoster

Biology

Molybdenum (Mo) is an essential trace metal found in most foods. Enzymes that require Mo cannot use this metal unless it is chelated with an organic complex called the Mo cofactor. MOCS1 is a gene that encodes an enzyme that catalyzes the first step in the synthesis of the Mo Cofactor (“MoCo”). The MOCS1 gene is extremely highly conserved, found in bacteria, fungi, plants and animals. Mutations in MOCS1 cause a disease in humans known as Molybdenum cofactor (MoCo) deficiency, which ultimately results in a combined deficiency of three essential enzymatic functions that depend on Mo: sulfite oxidase, xanthine dehydrogenase and aldehyde oxidase. These enzymes confer a protective function on the cell, by removing toxic catabolites. Sulfite oxidase, for example, is located in the mitochondrial intermembrane space, where it catalyzes the oxidation of sulfite to sulfate, removing the reactive and potentially toxic sulfite from the cell. MoCo deficiency segregates as an autosomal recessive disorder, and generally leads to early childhood death. We hypothesize that an increase in MOCS1 gene expression may have protective effects, by permitting the enzymes that depend on Mo and its cofactor to function more efficiently. Life extending strategies in model organisms have been successful when targeting similar protective pathways that also involve mitochondrial function. The work presented here outlines the preparatory phase of a longevity experiment, in which we plan to upregulate MOCS1 gene expression in fruit flies, and measure the effect on lifespan.