Crucial role of the Rcl1p-Bms1p interaction for yeast pre-ribosomal RNA processing.
Nucleic Acids Res
; 42(15): 10161-72, 2014 Sep.
Article
em En
| MEDLINE
| ID: mdl-25064857
ABSTRACT
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 Å 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.
Texto completo:
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Base de dados:
MEDLINE
Assunto principal:
RNA Ribossômico
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Proteínas Nucleares
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Processamento Pós-Transcricional do RNA
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Proteínas de Ligação a RNA
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Proteínas de Ligação ao GTP
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Proteínas de Saccharomyces cerevisiae
Idioma:
En
Ano de publicação:
2014
Tipo de documento:
Article