NDLI: Association of RNase mitochondrial RNA processing enzyme with ribonuclease P in higher ordered structures in the nucleolus: a possible coordinate role in ribosome biogenesis.

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Association of RNase mitochondrial RNA processing enzyme with ribonuclease P in higher ordered structures in the nucleolus: a possible coordinate role in ribosome biogenesis.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Craft, J. Lee, B. Ward, D. C. Matera, A. G.
Description	Author Affiliation: Lee B ( Department of Internal Medicine, Yale University School of Medicine, New Haven, CT 06520-8031, USA.);
Abstract	RNase mitochondrial RNA processing enzyme (MRP) is a nucleolar ribonucleoprotein particle that participates in 5.8S ribosomal RNA maturation in eukaryotes. This enzyme shares a polypeptide and an RNA structural motif with ribonuclease P (RNase P), a nuclear endoribonuclease originally described in the nucleus that processes RNA transcripts to generate their mature 5' termini. Both enzymes are also located in mitochondria. This report further characterizes the relationship between RNase MRP and RNase P. Antisense affinity selection with biotinylated 2'-O-methyl oligoribonucleotides and glycerol gradient fractionation experiments demonstrated that small subpopulations of RNase MRP and RNase P associate with each other in vivo in macromolecular complex, possibly 60-80S preribosomes. This latter notion was supported by fluorescence in situ hybridization experiments with antisense oligonucleotides that localized that RNA components of RNase MRP and RNase P to the nucleolus and to discrete cytoplasmic structures. These findings suggest that small subpopulations of RNase MRP and RNase P are physically associated, and that both may function in ribosomal RNA maturation or ribosome assembly.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	21
Volume Number	93
Language	English
Publisher	National Academy of Sciences
Publisher Date	1996-12-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Cell Nucleolus Metabolism Endoribonucleases Chemistry Nucleic Acid Conformation RNA, Catalytic Ribosomes Chromatography, Affinity Isolation & Purification HeLa Cells In Situ Hybridization Mitochondria Molecular Sequence Data RNA, Ribosomal, 5.8S Ribonuclease H Ribonuclease P Ribonucleoproteins Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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