Abstract
The four nucleolar proteins NOP1, SSB1, GAR1, and NSR1 of Saccharomyces cerevisiae share a repetitive domain composed of repeat units rich in glycine and arginine (GAR domain). We have cloned and sequenced a fifth member of this family, NOP3, and shown it to be essential for cell viability. The NOP3 open reading frame encodes a 415 amino acid protein with a predicted molecular mass of 45 kD, containing a GAR domain and an RNA recognition motif. NOP3-specific antibodies recognize a 60-kD protein by SDS-PAGE and decorate the nucleolus and the surrounding nucleoplasm. A conditional lethal mutation, GAL::nop3, was constructed; growth of the mutant strain in glucose medium represses NOP3 expression. In cells depleted of NOP3, production of cytoplasmic ribosomes is impaired. Northern analysis and pulse-chase labeling indicate that pre-rRNA processing is inhibited at the late steps, in which 27SB pre-rRNA is cleaved to 25S rRNA and 20S pre-rRNA to 18S rRNA.
MeSH Terms
Amino Acid Sequence
Base Sequence
Cell Nucleolus/chemistry
Cell Nucleus/chemistry
Cloning, Molecular
Fluorescent Antibody Technique
Fungal Proteins/chemistry,genetics,metabolism
Molecular Sequence Data
Molecular Weight
Mutation
Nuclear Proteins/chemistry,genetics,metabolism
RNA Precursors/metabolism
RNA Processing, Post-Transcriptional
RNA, Fungal/metabolism
RNA-Binding Proteins
Ribosomes/metabolism
Saccharomyces cerevisiae/chemistry,genetics,physiology
Saccharomyces cerevisiae Proteins
Chemicals
Fungal Proteins
NPL3 protein, S cerevisiae
Nuclear Proteins
RNA Precursors
RNA, Fungal
RNA-Binding Proteins
Saccharomyces cerevisiae Proteins
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Russell I D
European Molecular Biology Laboratory, Heidelberg, Germany.
Tollervey D
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