Evolution from DNA to RNA recognition by the bI3 LAGLIDADG maturase |
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Authors: | Longo Antonella Leonard Christopher W Bassi Gurminder S Berndt Daniel Krahn Joseph M Hall Traci M Tanaka Weeks Kevin M |
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Institution: | Department of Chemistry, University of North Carolina, Chapel Hill, North Carolina 27599-3290, USA. |
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Abstract: | LAGLIDADG endonucleases bind across adjacent major grooves via a saddle-shaped surface and catalyze DNA cleavage. Some LAGLIDADG proteins, called maturases, facilitate splicing by group I introns, raising the issue of how a DNA-binding protein and an RNA have evolved to function together. In this report, crystallographic analysis shows that the global architecture of the bI3 maturase is unchanged from its DNA-binding homologs; in contrast, the endonuclease active site, dispensable for splicing facilitation, is efficiently compromised by a lysine residue replacing essential catalytic groups. Biochemical experiments show that the maturase binds a peripheral RNA domain 50 A from the splicing active site, exemplifying long-distance structural communication in a ribonucleoprotein complex. The bI3 maturase nucleic acid recognition saddle interacts at the RNA minor groove; thus, evolution from DNA to RNA function has been mediated by a switch from major to minor groove interaction. |
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