Structure of a tyrosyl-tRNA synthetase splicing factor bound to a group I intron RNA

Paul J. Paukstelis, Jui-Hui Chen, Elaine Chase, Alan M. Lambowitz () and Barbara L. Golden ()
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Paul J. Paukstelis: Institute for Cellular and Molecular Biology, and Section of Molecular Genetics and Microbiology, School of Biological Sciences, University of Texas at Austin, Austin, Texas 78712, USA
Jui-Hui Chen: Purdue University, West Lafayette, Indiana 47907, USA
Elaine Chase: Purdue University, West Lafayette, Indiana 47907, USA
Alan M. Lambowitz: Institute for Cellular and Molecular Biology, and Section of Molecular Genetics and Microbiology, School of Biological Sciences, University of Texas at Austin, Austin, Texas 78712, USA
Barbara L. Golden: Purdue University, West Lafayette, Indiana 47907, USA

Nature, 2008, vol. 451, issue 7174, 94-97

Abstract: Old world order Life on Earth is believed to have evolved from an 'RNA world' where RNA molecules both catalysed essential chemical reactions and carried genetic information. In modern biology, proteins have become the enzymatic workhorses of the cell, while nucleic acids retain the informational role. Within cells, however, relics of the RNA world remain. One such is the mitochondrial tyrosyl-tRNA synthetase, CYT-18, from the fungus Neurospora crassa, which also binds a group I intron ribozyme and facilitates splicing. The crystal structure of this protein/ribozyme complex has now been determined. The interaction surface is different from that used by CYT-18 to bind tRNATyr in its enzymic role. Specific changes are found which do not exist in non-splicing tRNA synthetases, suggesting ways in which RNA–protein complexes could have evolved from RNA-only enzymes.

Date: 2008
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DOI: 10.1038/nature06413

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