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Access through your institution Buy or subscribe > splice variants abrogated the ... catalytic domain but retained ... > the later-gained domains The authors carried out a
comprehensive search for alternative splice variants of 37 human aaRSs in brain tissues and in leukocytes, using gene-specific multiplex PCR of exon–exon junctions, followed by deep
sequencing. They discovered hundreds of novel splice variants and, surprisingly, found that 60 of the 70 identified internal in-frame splice variants abrogated the highly conserved catalytic
domain but retained at least one of the later-gained domains. These variants are therefore catalytic nulls in regard to the canonical function of aaRSs, but they may have other biological
functions. In support of this, the observed loss of specific exons could potentially lead to extensive structural changes and thus create new protein interactions. This is a preview of
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ADDITIONAL ACCESS OPTIONS: * Log in * Learn about institutional subscriptions * Read our FAQs * Contact customer support REFERENCES * Lo, W.-S. et al. Human tRNA synthetase catalytic nulls
with diverse functions. _Science_ 345, 328–332 (2014) Article CAS PubMed PubMed Central Google Scholar Download references Authors * Eytan Zlotorynski View author publications You can
also search for this author inPubMed Google Scholar RELATED LINKS RELATED LINKS RELATED LINKS IN NATURE RESEARCH Guo, M., Yang, X.-L. & Schimmel, S. New functions of aminoacyl-tRNA
synthetases beyond translation. _Nature Rev. Mol. Cell Biol._ 11, 668–674 (2010) RIGHTS AND PERMISSIONS Reprints and permissions ABOUT THIS ARTICLE CITE THIS ARTICLE Zlotorynski, E.
Catalytic nulls keep busy. _Nat Rev Mol Cell Biol_ 15, 563 (2014). https://doi.org/10.1038/nrm3856 Download citation * Published: 06 August 2014 * Issue Date: September 2014 * DOI:
https://doi.org/10.1038/nrm3856 SHARE THIS ARTICLE Anyone you share the following link with will be able to read this content: Get shareable link Sorry, a shareable link is not currently
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