1UOC

X-Ray Structure and Activity of the Yeast Pop2 Protein: A Nuclease Subunit of the Mrna Deadenylase Complex

(2003) EMBO Rep 4: 1150

• PubMed: 14618157 Search on PubMedSearch on PubMed Central
• DOI: https://doi.org/10.1038/sj.embor.7400020
• Primary Citation of Related Structures:  
  1UOC


• PubMed Abstract: 
  

  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 A 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.

   View More

---

Organizational Affiliation: 

European Molecular Biology Laboratory, Meyerhofstrasse 1, D-69117 Heidelberg, Germany.