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Structural insight into precursor ribosomal RNA processing by ribonuclease MRP

Pengfei Lan1,2, Bin Zhou1,2, Ming Tan1,2

  • 1State Key Laboratory of Oncogenes and Related Genes, Ninth People's Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai 200011, China.

Science (New York, N.Y.)
|June 27, 2020
PubMed

Insights

Researchers uncovered how Ribonuclease MRP (RNase MRP) recognizes diverse RNA substrates. Coevolution of its protein and RNA components enables it to process single-stranded RNAs, suggesting many undiscovered roles.

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Structural Biology

Background:

  • Ribonuclease MRP (RNase MRP) is a crucial ribonucleoprotein complex in eukaryotes.
  • It is involved in precursor ribosomal RNA (pre-rRNA) processing and cell cycle regulation.
  • The mechanism of RNase MRP substrate recognition remained unclear, unlike the well-understood RNase P.

Purpose of the Study:

  • To elucidate the substrate recognition mechanism of RNase MRP.
  • To understand how RNase MRP interacts with its RNA targets.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) was used to determine the structures of Saccharomyces cerevisiae RNase MRP.
  • Structures were obtained for the enzyme alone and in complex with a pre-rRNA fragment.
  • Biochemical studies were conducted to complement structural data.

Main Results:

  • The study determined the cryo-EM structures of RNase MRP.
  • Structural and biochemical data revealed that RNase MRP recognizes single-stranded RNAs via a short, flexible consensus sequence.
  • Coevolution of protein and RNA subunits was identified as key to its function.

Conclusions:

  • RNase MRP has evolved into a distinct ribonuclease with broad substrate specificity.
  • Its ability to recognize a loosely defined sequence suggests numerous, yet undiscovered, RNA substrates.
  • These findings open new avenues for investigating RNase MRP's roles in cellular processes.

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