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Cryo-EM structure of catalytic ribonucleoprotein complex RNase MRP
by
Berezin, Igor
, Perederina, Anna
, Lee, Hyunwook
, Krasilnikov, Andrey S.
, Li, Di
, Hafenstein, Susan L.
, Bator, Carol
in
101/28
/ 631/337/1910
/ 631/337/384
/ 631/45/500
/ 631/45/535/1258/1259
/ Carbon - chemistry
/ Catalysis
/ Catalytic Domain
/ Cell cycle
/ Cellular structure
/ Cryoelectron Microscopy
/ Divergence
/ Endoribonucleases - ultrastructure
/ Humanities and Social Sciences
/ Humans
/ Material requirements planning
/ Maturation
/ Models, Molecular
/ multidisciplinary
/ Nucleic Acid Conformation
/ Protein Conformation
/ Proteins
/ Ribonuclease MRP
/ Ribonuclease P
/ Ribonuclease P - chemistry
/ Ribonucleoproteins - ultrastructure
/ RNA, Catalytic - chemistry
/ RNA, Fungal - chemistry
/ rRNA
/ Saccharomyces cerevisiae
/ Saccharomyces cerevisiae - enzymology
/ Science
/ Science (multidisciplinary)
2020
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Cryo-EM structure of catalytic ribonucleoprotein complex RNase MRP
by
Berezin, Igor
, Perederina, Anna
, Lee, Hyunwook
, Krasilnikov, Andrey S.
, Li, Di
, Hafenstein, Susan L.
, Bator, Carol
in
101/28
/ 631/337/1910
/ 631/337/384
/ 631/45/500
/ 631/45/535/1258/1259
/ Carbon - chemistry
/ Catalysis
/ Catalytic Domain
/ Cell cycle
/ Cellular structure
/ Cryoelectron Microscopy
/ Divergence
/ Endoribonucleases - ultrastructure
/ Humanities and Social Sciences
/ Humans
/ Material requirements planning
/ Maturation
/ Models, Molecular
/ multidisciplinary
/ Nucleic Acid Conformation
/ Protein Conformation
/ Proteins
/ Ribonuclease MRP
/ Ribonuclease P
/ Ribonuclease P - chemistry
/ Ribonucleoproteins - ultrastructure
/ RNA, Catalytic - chemistry
/ RNA, Fungal - chemistry
/ rRNA
/ Saccharomyces cerevisiae
/ Saccharomyces cerevisiae - enzymology
/ Science
/ Science (multidisciplinary)
2020
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Cryo-EM structure of catalytic ribonucleoprotein complex RNase MRP
by
Berezin, Igor
, Perederina, Anna
, Lee, Hyunwook
, Krasilnikov, Andrey S.
, Li, Di
, Hafenstein, Susan L.
, Bator, Carol
in
101/28
/ 631/337/1910
/ 631/337/384
/ 631/45/500
/ 631/45/535/1258/1259
/ Carbon - chemistry
/ Catalysis
/ Catalytic Domain
/ Cell cycle
/ Cellular structure
/ Cryoelectron Microscopy
/ Divergence
/ Endoribonucleases - ultrastructure
/ Humanities and Social Sciences
/ Humans
/ Material requirements planning
/ Maturation
/ Models, Molecular
/ multidisciplinary
/ Nucleic Acid Conformation
/ Protein Conformation
/ Proteins
/ Ribonuclease MRP
/ Ribonuclease P
/ Ribonuclease P - chemistry
/ Ribonucleoproteins - ultrastructure
/ RNA, Catalytic - chemistry
/ RNA, Fungal - chemistry
/ rRNA
/ Saccharomyces cerevisiae
/ Saccharomyces cerevisiae - enzymology
/ Science
/ Science (multidisciplinary)
2020
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Cryo-EM structure of catalytic ribonucleoprotein complex RNase MRP
Journal Article
Cryo-EM structure of catalytic ribonucleoprotein complex RNase MRP
2020
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Overview
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 some of the RNase MRP proteins shared with RNase P undergo an unexpected RNA-driven remodeling that allows them to bind to divergent RNAs. Further, we reveal how this RNA-driven protein remodeling, acting together with the introduction of new auxiliary elements, results in the functional diversification of RNase MRP and its progenitor, RNase P, and demonstrate structural underpinnings of the acquisition of new functions by catalytic RNPs.
Ribozyme-based RNase MRP is an essential eukaryotic enzyme involved in the maturation of rRNA and is evolutionarily related to RNase P. Here, the authors present the 3.0 Å cryo-EM structure of the
S. cerevisiae
RNase MRP holoenzyme, a 450 kDa ribonucleoprotein complex and compare it with RNase P.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
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