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Literature summary for 3.1.13.1 extracted from

  • Lorentzen, E.; Basquin, J.; Tomecki, R.; Dziembowski, A.; Conti, E.
    Structure of the active subunit of the yeast exosome core, Rrp44: diverse modes of substrate recruitment in the RNase II nuclease family (2008), Mol. Cell, 29, 717-728.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
full-length Rrp44 (residues 1-1001) and truncated constructs of Rrp44 expressed from a pETM11 vector in Escherichia coli Saccharomyces cerevisiae

Crystallization (Commentary)

Crystallization (Comment) Organism
Rrp44 in complex with single-stranded RNA, to 2.3 A resolution. Structure of Rrp44 displays CSD1, CSD2, RNB, and S1 domains. The two N-terminal cold shock domains (CSD1, residues 271-399; CSD2, residues 400-475) and the C-terminal S1 domain (residues 911-998) display characteristic OB folds, with five antiparallel beta strands organized in a beta barrel structure. CSD1 is fused to an N-terminal alpha helix (residues 261-268) and the S1 domain has an insertion of three beta strands (between beta3 and beta4) as compared to a standard OB fold. The RNB domain is centered around a core and is surrounded by several alpha helices Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
A815F degrades RNA duplexes with 7 or 14 nucleotides of ssRNA overhang significantly slower (about 4fold) than the wild-type enzyme Saccharomyces cerevisiae
A815W degrades RNA duplexes with 7 or 14 nucleotides of ssRNA overhang significantly slower (about 3fold) than the wild-type enzyme Saccharomyces cerevisiae
D551N abolishes the exonucleolytic activity Saccharomyces cerevisiae
additional information Rrp44 242-1001 (Rrp44DELTAN) lacks the predicted N-terminal PIN domain, shows no detectable difference in activity toward ssRNA substrates as compared to recombinant Rrp44 Saccharomyces cerevisiae

Localization

Localization Comment Organism GeneOntology No. Textmining
additional information exosome, i.e. a macromolecule complex involved in RNA degradation Saccharomyces cerevisiae
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Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae Q08162
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Purification (Commentary)

Purification (Comment) Organism
full-length protein and mutants purified by affinity Ni-NTA chromatography, followed by ion exchange chromatography and gel filtration. 242-1001 construct purified to homogeneity Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dsRNA + H2O Rrp44 is very efficient in degrading a duplex with a 30 overhang of 14 nucleotides and is inactive with overhangs as short as 2 or 3 nucleotides Saccharomyces cerevisiae ?
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ssRNA + H2O 50fold higher affinity for ssRNA than for a corresponding ssDNA oligonucleotide Saccharomyces cerevisiae ?
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Synonyms

Synonyms Comment Organism
Rrp44
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Saccharomyces cerevisiae