Crystal structure of group II intron domain 1 reveals a template for RNA assembly
[3];
- Yale Univ., New Haven, CT (United States). Dept. of Molecular Biophysics and Biochemistry
- Argonne National Lab. (ANL), Argonne, IL (United States). Northeastern Collaborative Access Team (NE-CAT); Cornell Univ., Ithaca, NY (United States). Dept. of Chemistry and Chemical Biology
- Yale Univ., New Haven, CT (United States). Dept. of Molecular, Cellular, and Developmental Biology
- Yale Univ., New Haven, CT (United States). Dept. of Molecular, Cellular, and Developmental Biology. Dept. of Chemistry; Howard Hughes Medical Inst., Chevy Chase, MD (United States)
Although the importance of large noncoding RNAs is increasingly appreciated, our understanding of their structures and architectural dynamics remains limited. In particular, we know little about RNA folding intermediates and how they facilitate the productive assembly of RNA tertiary structures. In this paper, we report the crystal structure of an obligate intermediate that is required during the earliest stages of group II intron folding. Composed of domain 1 from the Oceanobacillus iheyensis group II intron (266 nucleotides), this intermediate retains native-like features but adopts a compact conformation in which the active site cleft is closed. Transition between this closed and the open (native) conformation is achieved through discrete rotations of hinge motifs in two regions of the molecule. Finally, the open state is then stabilized by sequential docking of downstream intron domains, suggesting a 'first come, first folded' strategy that may represent a generalizable pathway for assembly of large RNA and ribonucleoprotein structures.
- Research Organization:
- Yale Univ., New Haven, CT (United States); Argonne National Lab. (ANL), Argonne, IL (United States)
- Sponsoring Organization:
- USDOE Office of Science (SC); National Inst. of Health (NIH) (United States)
- Contributing Organization:
- Howard Hughes Medical Inst., Chevy Chase, MD (United States); Cornell Univ., Ithaca, NY (United States)
- Grant/Contract Number:
- AC02-06CH11357; RO1GM50313; P41 GM103403; S10 RR029205
- OSTI ID:
- 1227028
- Journal Information:
- Nature Chemical Biology, Vol. 11, Issue 12; ISSN 1552-4450
- Publisher:
- Nature Publishing GroupCopyright Statement
- Country of Publication:
- United States
- Language:
- ENGLISH
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