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A conserved element in the yeast RNase MRP RNA subunit can participate in a long-range base-pairing interaction

Scott C Walker1, Johanna M Avis

  • 1Department of Biomolecular Sciences, UMIST, P.O. Box 88, Manchester, M60 1QD, UK.

Journal of Molecular Biology
|July 28, 2004
PubMed

Insights

Researchers identified a new stem in yeast RNase MRP RNA, increasing its similarity to RNase P RNA. This stem, while not essential for function, may play a role in enzyme assembly.

Area of Science:

  • Molecular Biology
  • Biochemistry
  • RNA Structure

Background:

  • RNase MRP is a crucial enzyme for eukaryotic pre-ribosomal RNA (pre-rRNA) processing.
  • Its RNA subunit shares structural similarities with RNase P RNA, suggesting a common evolutionary origin or functional relationship.

Purpose of the Study:

  • To conduct a comprehensive structural analysis of Saccharomyces cerevisiae MRP RNA.
  • To investigate the implications of a newly identified stem on the overall RNA structure and its relation to RNase P RNA.

Main Methods:

  • Enzymatic and chemical probing of yeast MRP RNA.
  • Site-directed mutagenesis to alter RNA structure.
  • Thermal melting assays to assess RNA stability.
  • Sequence analysis of known yeast MRP RNA.

Main Results:

  • A previously unrecognized stem, analogous to the P7 stem of RNase P, was identified in yeast MRP RNA.
  • This P7-like stem enhances structural similarity to RNase P RNA and refines the boundaries of domain 2, the proposed specificity domain.
  • The stem formation involves a conserved sequence element (ymCR-II) and is potentially present in various yeast MRP RNA sequences.
  • Formation of this stem is not essential for RNase MRP's pre-rRNA processing or overall function.
  • Mutants forming the stem impair RNase MRP function, suggesting in vivo formation but requiring specific pairing for activity.

Conclusions:

  • The identified P7-like stem contributes to a more detailed understanding of yeast MRP RNA structure and its relationship with RNase P RNA.
  • While not part of the active enzyme, this alternative structure is more stable in the absence of proteins and may represent an intermediate in RNase MRP assembly.

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