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Nop53p interacts with 5.8S rRNA co‐transcriptionally, and regulates processing of pre‐rRNA by the exosome
Author(s) -
Granato Daniela C.,
MachadoSantelli Glaucia M.,
Oliveira Carla C.
Publication year - 2008
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/j.1742-4658.2008.06565.x
Subject(s) - ribosomal rna , biology , ribosomal protein , ribosome , polyadenylation , microbiology and biotechnology , 23s ribosomal rna , rna , genetics , gene
In eukaryotes, pre‐rRNA processing depends on a large number of nonribosomal trans ‐acting factors that form intriguingly organized complexes. One of the early stages of pre‐rRNA processing includes formation of the two intermediate complexes pre‐40S and pre‐60S, which then form the mature ribosome subunits. Each of these complexes contains specific pre‐rRNAs, ribosomal proteins and processing factors. The yeast nucleolar protein Nop53p has previously been identified in the pre‐60S complex and shown to affect pre‐rRNA processing by directly binding to 5.8S rRNA, and to interact with Nop17p and Nip7p, which are also involved in this process. Here we show that Nop53p binds 5.8S rRNA co‐transcriptionally through its N‐terminal region, and that this protein portion can also partially complement growth of the conditional mutant strain Δ nop53/GAL::NOP53 . Nop53p interacts with Rrp6p and activates the exosome in vitro . These results indicate that Nop53p may recruit the exosome to 7S pre‐rRNA for processing. Consistent with this observation and similar to the observed in exosome mutants, depletion of Nop53p leads to accumulation of polyadenylated pre‐rRNAs.