Dim2p, a KH-domain protein required for small ribosomal subunit synthesis
Open Access
- 22 March 2004
- journal article
- Published by Cold Spring Harbor Laboratory in RNA
- Vol. 10 (4) , 645-656
- https://doi.org/10.1261/rna.5162204
Abstract
Recent proteomic analyses are revealing the dynamics of preribosome assembly. Following cleavage at processing site A2, which generates the 20S pre-rRNA (the immediate precursor to the 18S rRNA), early RRPs (ribosomal RNA processing factors) are released in bulk from the preribosomes, and the resulting pre-40S subunits are left associated with a limited set of proteins that we refer to as the SSU RRP complex. Dim2p, a core constituent of the SSU RRP complex and conserved KH-domain containing protein, is required for pre-rRNA processing and is associated with early nucleolar and late cytoplasmic pre-rRNA species. Consistently, Dim2p shuttles between the nucle(ol)us and the cytoplasm, a trafficking that is tightly regulated by growth. The association of Dim2p with the 18S rRNA dimethyltransferase Dim1p, as well as its requirement for pre-rRNA processing at cleavage sites A1 and A2 and for 18S rRNA dimethylation, suggest that Dim2p may recruit Dim1p to nucleolar pre-rRNAs through its KH domain.Keywords
This publication has 53 references indexed in Scilit:
- Global protein function prediction from protein-protein interaction networksNature Biotechnology, 2003
- Nob1p Is Required for Cleavage of the 3′ End of 18S rRNAMolecular and Cellular Biology, 2003
- Real-Time Visualization of ZBP1 Association with β-Actin mRNA during Transcription and LocalizationCurrent Biology, 2003
- Chromosomal gradient of histone acetylation established by Sas2p and Sir2p functions as a shield against gene silencingNature Genetics, 2002
- Small Nucleolar RNAsCell, 2002
- Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometryNature, 2002
- Functional organization of the yeast proteome by systematic analysis of protein complexesNature, 2002
- KH domains within the FMR1 sequence suggest that fragile X syndrome stems from a defect in RNA metabolismTrends in Biochemical Sciences, 1993
- A point mutation in the FMR-1 gene associated with fragile X mental retardationNature Genetics, 1993
- Ribosomal precursor particles from yeastExperimental Cell Research, 1975