New research led by scientists at The Scripps Research Institute (TSRI) reveals that a human enzyme has changed little from its days as a bacterial enzyme. In fact, the enzyme appears to be unique in its ability to change its shape–and its job in cells — without overhauling its basic architecture.
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Schimmel and his colleagues focused on a member of a family of enzymes called aminoacyl tRNA synthetases….
“Aminoacyl tRNA synthetases are associated with–and we believe needed for — the building of organismal complexity, such as making tissues and organs in humans,” Schimmel explained.
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These new functions are controlled by “decorations,” or additions to the aminoacyl tRNA synthetase architecture, which are generally lacking in bacteria; however, there is one aminoacyl tRNA synthetase, called AlaRS, that lacks any new decorations. AlaRS somehow carries out new roles in humans using a preexisting bacterial domain in its structure….
The scientists…showed that a domain of AlaRS’s structure, called C-Ala, had been reshaped to take on a new role in humans. The end result is the same as if AlaRS had gained a new decoration….
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