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Structure and function of archaeal box C/D sRNP core proteins

Nature Structural & Molecular Biology volume 10, pages 256–263 (2003)Cite this article

Abstract

Nop56p and Nop58p are two core proteins of the box C/D snoRNPs that interact concurrently with fibrillarin and snoRNAs to function in enzyme assembly and catalysis. Here we report the 2.9 Å resolution co-crystal structure of an archaeal homolog of Nop56p/Nop58p, Nop5p, in complex with fibrillarin from Archaeoglobus fulgidus (AF) and the methyl donor S-adenosyl-L-methionine. The N-terminal domain of Nop5p forms a complementary surface to fibrillarin that serves to anchor the catalytic subunit and to stabilize cofactor binding. A coiled coil in Nop5p mediates dimerization of two fibrillarin–Nop5p heterodimers for optimal interactions with bipartite box C/D RNAs. Structural analysis and complementary biochemical data demonstrate that the conserved C-terminal domain of Nop5p harbors RNA-binding sites. A model of box C/D snoRNP assembly is proposed based on the presented structural and biochemical data.

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Figure 1: Crystal structure of the AF fibrillarin–Nop5p complex.
Figure 2: Sequence alignment of AF Nop5p against its homologs retrieved from SWISS-PROT database (http://us.expasy.org/sprot/).
Figure 3: The fibrillarin–Nop5p interface.
Figure 4: Dissecting the functions of Nop5p domains.
Figure 5: The C-terminal domain of Nop5p is important for binding to box C/D RNA.
Figure 6: AdoMet binding to fibrillarin.
Figure 7: A proposed model of archaeal box C/D snoRNP assembly.

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Acknowledgements

We thank T. Somasundaram and J. Hildenbrand for assistance with data collection, C. Ogata for beamtime allocation at the Brookhaven National Laboratory and National Synchrotron Light Source, and E.K.H. Allen and M. Jackson for reading the manuscript. This work was supported in part by a grant from the Florida Department of Health to H.L.

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  1. Department of Chemistry and Biochemistry, Institute of Molecular Biophysics, Florida State University, Tallahassee, 32306, Florida, USA

    Mohamed Aittaleb, Rumana Rashid, Qiong Chen & Hong Li

  2. Department of Microbiology, The Ohio State University, Columbus, 43210, Ohio, USA

    John R. Palmer & Charles J. Daniels

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Correspondence to Hong Li.

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Aittaleb, M., Rashid, R., Chen, Q. et al. Structure and function of archaeal box C/D sRNP core proteins. Nat Struct Mol Biol 10, 256–263 (2003). https://doi.org/10.1038/nsb905

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