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Literature summary for 3.1.13.4 extracted from

  • Mangus, D.A.; Evans, M.C.; Agrin, N.S.; Smith, M.; Gongidi, P.; Jacobson, A.
    Positive and negative regulation of poly(A) nuclease (2004), Mol. Cell. Biol., 24, 5521-5533.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.13.4

Cloned(Commentary)

Cloned (Comment) Organism
expression of enzyme subunits in the two-hybrid system using strain L40, expression of lexA-tagged wild-type and mutant Pab1p, Pan2p, and Pan3p in Escherichia coli, expression of full-length and N-terminal constructs of factor Pbp1p in Escherichia coli, overview Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
A519V site-directed mutagenesis of Pab1p, the mutant shows no resistance to 3-AT in contrast to the wild-type protein, identification of interaction residues and domains with Ppb1p, Pan2p and Pan3p Saccharomyces cerevisiae
G444D site-directed mutagenesis of Pab1p, the mutant shows no resistance to 3-AT in contrast to the wild-type protein, identification of interaction residues and domains with Ppb1p, Pan2p and Pan3p Saccharomyces cerevisiae
G528D site-directed mutagenesis of Pab1p, the mutant shows no resistance to 3-AT in contrast to the wild-type protein, identification of interaction residues and domains with Ppb1p, Pan2p and Pan3p Saccharomyces cerevisiae
additional information growth of cells transformed with mutant constructs, overview Saccharomyces cerevisiae
R506G site-directed mutagenesis of Pab1p, the mutant shows no resistance to 3-AT in contrast to the wild-type protein, identification of interaction residues and domains with Ppb1p, Pan2p and Pan3p Saccharomyces cerevisiae
V451A site-directed mutagenesis of Pab1p, the mutant shows no resistance to 3-AT in contrast to the wild-type protein, identification of interaction residues and domains with Ppb1p, Pan2p and Pan3p Saccharomyces cerevisiae
Y514C site-directed mutagenesis of Pab1p, the mutant shows reduced resistance to 3-AT compared to the wild-type protein, identification of interaction residues and domains with Ppb1p, Pan2p and Pan3p Saccharomyces cerevisiae

Inhibitors

Inhibitors Comment Organism Structure
3-aminotriazole competitive inhibitor Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Saccharomyces cerevisiae the enzyme plays an important role in the posttranscriptional maturation of mRNA poly(A) tails, factors involved in positive, e.g. Pan3p, and negative, e.g. Pbp1p, regulation, schematic model, overview ?
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 ?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
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 strains L40 and yAS1255, a pab1DELTA strain, and a pan3DELTA strain yME43
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme plays an important role in the posttranscriptional maturation of mRNA poly(A) tails, factors involved in positive, e.g. Pan3p, and negative, e.g. Pbp1p, regulation, schematic model, overview Saccharomyces cerevisiae ?
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 ?
additional information protein-protein interaction specificity, Pab1p interacts with Pan3p and Pbp1p, which also interact with each other, Pbp1p interacts with itself, binding pocket structures, overview Saccharomyces cerevisiae ?
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 ?

Subunits

Subunits Comment Organism
More the enzyme requires the subunits Pan2p and Pan3p, as well as the poly(A)-binding protein Pab1p for activity Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
PAN
-
 Saccharomyces cerevisiae
poly(A) nuclease
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 Saccharomyces cerevisiae