Crucial role of the Rcl1p-Bms1p interaction for yeast pre-ribosomal RNA processing.
The essential Rcl1p and Bms1p proteins form a complex required for 40S ribosomal subunit maturation. Bms1p is a GTPase and Rcl1p has been proposed to catalyse the endonucleolytic cleavage at site A2 separating the pre-40S and pre-60S maturation pathways. We determined the 2.0 A crystal structure of Bms1p associated with ... Rcl1p. We demonstrate that Rcl1p nuclear import depends on Bms1p and that the two proteins are loaded into pre-ribosomes at a similar stage of the maturation pathway and remain present within pre-ribosomes after cleavage at A2. Importantly, GTP binding to Bms1p is not required for the import in the nucleus nor for the incorporation of Rcl1p into pre-ribosomes, but is essential for early pre-rRNA processing. We propose that GTP binding to Bms1p and/or GTP hydrolysis may induce conformational rearrangements within the Bms1p-Rcl1p complex allowing the interaction of Rcl1p with its RNA substrate.
Mesh Terms:
Active Transport, Cell Nucleus, Cell Nucleus, GTP-Binding Proteins, Gene Expression Regulation, Fungal, Guanosine Triphosphate, Nuclear Proteins, Point Mutation, Protein Binding, Protein Interaction Domains and Motifs, RNA Precursors, RNA Processing, Post-Transcriptional, RNA, Ribosomal, RNA-Binding Proteins, Ribosomes, Saccharomyces cerevisiae Proteins
Active Transport, Cell Nucleus, Cell Nucleus, GTP-Binding Proteins, Gene Expression Regulation, Fungal, Guanosine Triphosphate, Nuclear Proteins, Point Mutation, Protein Binding, Protein Interaction Domains and Motifs, RNA Precursors, RNA Processing, Post-Transcriptional, RNA, Ribosomal, RNA-Binding Proteins, Ribosomes, Saccharomyces cerevisiae Proteins
Nucleic Acids Res.
Date: Sep. 01, 2014
PubMed ID: 25064857
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