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PMID: 14657029 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Yeast Nop15p is an RNA-binding protein required for pre-rRNA processing and cytokinesis.

The EMBO journal ·Vol. 22 ·No. 24 ·2003-12-15 ·Pages 6573-83

Oeffinger M, Tollervey D

Abstract

Nop15p is an essential protein that contains an RNA recognition motif (RRM) and localizes to the nucleoplasm and nucleolus. Cells depleted of Nop15p failed to synthesize the 25S and 5.8S rRNA components of the 60S ribosomal subunit, and exonucleolytic 5' processing of 5.8S rRNA was strongly inhibited. Pre-rRNAs co-precipitated with tagged Nop15p confirmed its association with early pre-60S particles and Nop15p bound a pre-rRNA transcript in vitro. Nop15p-depleted cells show an unusually abrupt growth arrest prior to substantial depletion of ribosomal subunits. Following cell synchronization in mitosis, Nop15p-depleted cells undergo nuclear division with wild-type kinetics, activate the mitotic exit network and disassemble their mitotic spindle. However, they uniformly arrest at cytokinesis and fail to assemble a contractile actin ring at the bud neck. In dividing wild-type cells, segregation of nucleolar proteins to the daughter nuclei occurs after separation of the nucleoplasm. In these late mitotic cells, Nop15p was partially delocalized from the nucleolus to the nucleoplasm, consistent with a specific function in cell division in addition to its role in ribosome synthesis.

MeSH Terms
Base Sequence Binding Sites Cell Division/genetics Cell Survival DNA Primers Methyltransferases Nuclear Proteins/metabolism RNA Precursors/genetics RNA, Fungal/genetics RNA, Ribosomal/genetics RNA-Binding Proteins/genetics Saccharomyces cerevisiae/cytology,genetics,physiology Saccharomyces cerevisiae Proteins/metabolism
Chemicals
DNA Primers Nuclear Proteins RNA Precursors RNA, Fungal RNA, Ribosomal RNA-Binding Proteins Saccharomyces cerevisiae Proteins Methyltransferases NOP2 protein, S cerevisiae
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Oeffinger Marlene
Wellcome Trust Centre for Cell Biology, University of Edinburgh, Edinburgh EH9 3JR, UK. [email protected]
Tollervey David
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Article Info
Journal
The EMBO journal
Abbr.
EMBO J
ISSN
0261-4189
DOI
10.1093/emboj/cdg616
Email
[email protected]
Published
2003-12-15
Pages
6573-83
Language
English
Region
England
NLM ID
8208664
PMCID
PMC291811
Subset
IM
External Links
PubMed source DOI: 10.1093/emboj/cdg616 PMC Full Text View journal details
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