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Cryo-EM structure of catalytic ribonucleoprotein complex RNase MRP

Anna Perederina, Di Li, Hyunwook Lee, Carol Bator, Igor Berezin, Susan L. Hafenstein, Andrey S. Krasilnikov
doi: https://doi.org/10.1101/2020.03.17.996132
Anna Perederina
1Department of Biochemistry and Molecular Biology, Pennsylvania State University, University Park, PA 16802
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Di Li
1Department of Biochemistry and Molecular Biology, Pennsylvania State University, University Park, PA 16802
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Hyunwook Lee
1Department of Biochemistry and Molecular Biology, Pennsylvania State University, University Park, PA 16802
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Carol Bator
1Department of Biochemistry and Molecular Biology, Pennsylvania State University, University Park, PA 16802
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Igor Berezin
1Department of Biochemistry and Molecular Biology, Pennsylvania State University, University Park, PA 16802
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Susan L. Hafenstein
1Department of Biochemistry and Molecular Biology, Pennsylvania State University, University Park, PA 16802
2Department of Medicine, Pennsylvania State University, Hershey, PA 17033
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Andrey S. Krasilnikov
1Department of Biochemistry and Molecular Biology, Pennsylvania State University, University Park, PA 16802
3Center for RNA Biology, Pennsylvania State University, University Park, PA 16802
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  • For correspondence: ask11@psu.edu
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Abstract

RNase MRP is an essential eukaryotic ribonucleoprotein complex involved in the maturation of rRNA and the regulation of the cell cycle. RNase MRP is related to the ribozyme-based RNase P, but it has evolved to have distinct cellular roles. We report a cryo-EM structure of the S. cerevisiae RNase MRP holoenzyme solved to 3.0 Å. We describe the structure of this 450 kDa complex, interactions between its components, and the organization of its catalytic RNA. We show that while the catalytic center of RNase MRP is inherited from the ancestral enzyme RNase P, the substrate binding pocket of RNase MRP is significantly altered by the addition of unique RNA and protein elements, as well as by RNA-driven protein remodeling.

One Sentence Summary Changes in peripheral RNA elements and RNA-driven protein remodeling result in diversification of related catalytic RNPs

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Posted March 18, 2020.
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Cryo-EM structure of catalytic ribonucleoprotein complex RNase MRP
Anna Perederina, Di Li, Hyunwook Lee, Carol Bator, Igor Berezin, Susan L. Hafenstein, Andrey S. Krasilnikov
bioRxiv 2020.03.17.996132; doi: https://doi.org/10.1101/2020.03.17.996132
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Cryo-EM structure of catalytic ribonucleoprotein complex RNase MRP
Anna Perederina, Di Li, Hyunwook Lee, Carol Bator, Igor Berezin, Susan L. Hafenstein, Andrey S. Krasilnikov
bioRxiv 2020.03.17.996132; doi: https://doi.org/10.1101/2020.03.17.996132

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