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X‐ray structure and activity of the yeast Pop2 protein: a nuclease subunit of the mRNA deadenylase complex
Author(s) -
Thore Stéphane,
Mauxion Fabienne,
Séraphin Bertrand,
Suck Dietrich
Publication year - 2003
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1038/sj.embor.7400020
Subject(s) - rnase h , nuclease , rnase p , saccharomyces cerevisiae , rna , rnase ph , rnase mrp , biology , mutagenesis , genetics , biochemistry , chemistry , dna , yeast , mutation , gene
In Saccharomyces cerevisiae , a large complex, known as the Ccr4–Not complex, containing two nucleases, is responsible for mRNA deadenylation. One of these nucleases is called Pop2 and has been identified by similarity with PARN, a human poly(A) nuclease. Here, we present the crystal structure of the nuclease domain of Pop2 at 2.3 Å resolution. The domain has the fold of the DnaQ family and represents the first structure of an RNase from the DEDD superfamily. Despite the presence of two non‐canonical residues in the active site, the domain displays RNase activity on a broad range of RNA substrates. Site‐directed mutagenesis of active‐site residues demonstrates the intrinsic ability of the Pop2 RNase D domain to digest RNA. This first structure of a nuclease involved in the 3′–5′ deadenylation of mRNA in yeast provides information for the understanding of the mechanism by which the Ccr4–Not complex achieves its functions.