Armt1: a phoenix rises from the ashes.

Derek Hoelz

doi:10.18632/oncotarget.5964

Abstract

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Armt1: a phoenix rises from the ashes.

Highlights

In the mid 1960s scientists discovered an enzyme activity in pituitary extracts that hydrolyzed s-adenosyl methionine (AdoMet) leading to the generation of methanol
It is known that methylation of four specific glutamyl residues in chemoreceptors by CheR is required for adaption in chemotaxis for some bacterial species
In the early 1980s, O’Connor and Clarke challenged the idea that protein methylase II was involved in signaling events in eukaryotic cells when they discovered that the mammalian enzyme catalyzed the transfer of methyl groups from AdoMet not to glutamyl or aspartyl residues, but to damaged L-isoapartyl or D-aspartyl residues that occur spontaneously in aging proteins [3]

Summary

Introduction

In the mid 1960s scientists discovered an enzyme activity in pituitary extracts that hydrolyzed s-adenosyl methionine (AdoMet) leading to the generation of methanol. In 1977, Springer and Koshland, Jr. uncovered that a necessary component of the bacterial chemical sensing system and product of the CheR gene was a protein O-methyltransferase [2]. It is known that methylation of four specific glutamyl residues in chemoreceptors by CheR is required for adaption in chemotaxis for some bacterial species.

Results

Conclusion