Journal
SCIENCE
Volume 345, Issue 6194, Pages 328-332Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1252943
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Funding
- Innovation and Technology Fund from the Hong Kong Government [UIM181, UIM192, UIM199]
- National Foundation for Cancer Research
- NIH [R01CA92577, R01GM088278, R01NS085092, R01HG005717, R01GM100136]
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Genetic efficiency in higher organisms depends on mechanisms to create multiple functions from single genes. To investigate this question for an enzyme family, we chose aminoacyl tRNA synthetases (AARSs). They are exceptional in their progressive and accretive proliferation of noncatalytic domains as the Tree of Life is ascended. Here we report discovery of a large number of natural catalytic nulls (CNs) for each human AARS. Splicing events retain noncatalytic domains while ablating the catalytic domain to create CNs with diverse functions. Each synthetase is converted into several new signaling proteins with biological activities orthogonal to that of the catalytic parent. We suggest that splice variants with nonenzymatic functions may be more general, as evidenced by recent findings of other catalytically inactive splice-variant enzymes.
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