Steven Clarke, "Molecular Instability and Enzyme Missteps as Root Causes of Aging - What Can Be Done?"
Nov 12, 2012 (Mon) | 4:00 PM -6:00 PM
393 Serra Mall, Herrin T-175 : Stanford, CA
The age-dependent accumulation of altered biomolecules cannot be compatible with the full physiological capacity of cells if they lack function, have reduced function, or are toxic. These molecules can be generated by spontaneous chemical degradation reactions and by errors of metabolic function. In addition to well-known pathways of DNA repair and generalized protein degradation, an increasing number of pathways have been discovered recently for the “repair” or elimination of damaged proteins and small molecules. We report here our findings related to three such systems in yeast, worm, and mammalian systems. First, we have discovered a methyltransferase-dependent pathway that can convert spontaneously damaged (R,S)-S-adenosylmethionine to the physiologically active (S,S) form. Second, we have characterized an enzyme that participates in the “sanitization” of the sugar nucleotide pool to prevent the misincorporation of sugars into glycoconjugates resulting from metabolic errors in enzymes forming GDP-mannose. Finally, we show that the protein repair methytransferase that is responsible for unkinking spontaneously-damaged proteins at aspartyl and asparaginyl residues is linked to induction of stress-related proteins by changes in the insulin/insulin-like signaling system.
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