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- Title
Evolution from DNA to RNA recognition by the bI3 LAGLIDADG maturase.
- Authors
Longo, Antonella; Leonard, Christopher W; Bassi, Gurminder S; Berndt, Daniel; Krahn, Joseph M; Hall, Traci M Tanaka; Weeks, Kevin M
- 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 Å 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.
- Subjects
DNA; RNA; NUCLEIC acids; ENDONUCLEASES; NUCLEASES; RNA splicing
- Publication
Nature Structural & Molecular Biology, 2005, Vol 12, Issue 9, p779
- ISSN
1545-9993
- Publication type
Article
- DOI
10.1038/nsmb976