Accurate Processing of a Eukaryotic Precursor Ribosomal RNA by Ribonuclease MRP In vitro

Very few of the enzymes required for eukaryotic precursor ribosomal RNA (pre-rRNA) processing have been identified. Ribonuclease (RNase) MRP was characterized as a nuclease that cleaves mitochondrial replication primers, but it is predominantly nucleolar. Previous genetic evidence revealed that this...

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Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 1996-04, Vol.272 (5259), p.268-270
Main Authors: Lygerou, Zoi, Allmang, Christine, Tollervey, David, Séraphin, Bertrand
Format: Article
Language:English
Subjects:
Base Sequence
Biochemistry
Biological and medical sciences
Cell growth
Cell Nucleolus - enzymology
Endoribonucleases - isolation & purification
Endoribonucleases - metabolism
Enzymes
Fractions
Fundamental and applied biological sciences. Psychology
Genetics
Marginal revenue products
Microbial genetics
Molecular and cellular biology
Molecular genetics
Molecular Sequence Data
Proteins
Ribonucleic acid
Ribonucleoproteins - metabolism
Ribosomal RNA
RNA
RNA precursors
RNA Precursors - metabolism
RNA Processing, Post-Transcriptional
RNA, Ribosomal - metabolism
Saccharomyces cerevisiae
Saccharomyces cerevisiae - enzymology
Transcription. Transcription factor. Splicing. Rna processing
Transcripts (Written Records)
Transfer RNA
Yeast
Yeasts
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Summary:Very few of the enzymes required for eukaryotic precursor ribosomal RNA (pre-rRNA) processing have been identified. Ribonuclease (RNase) MRP was characterized as a nuclease that cleaves mitochondrial replication primers, but it is predominantly nucleolar. Previous genetic evidence revealed that this ribonucleoprotein is required, directly or indirectly, for cleavage of the yeast pre-rRNA in vivo at site A$_3$. Here, an in vitro processing system that accurately reproduces this cleavage is described. Biochemical purification and the use of extracts depleted of the MRP RNA demonstrate that endonucleolytic cleavage of the pre-rRNA is directly mediated by RNase MRP. This establishes a role for RNase MRP in the nucleolus.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.272.5259.268