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Literature summary for 4.6.1.19 extracted from

  • Shcherbik, N.
    Golgi-mediated glycosylation determines residency of the T2 RNase Rny1p in Saccharomyces cerevisiae (2013), Traffic, 14, 1209-1227.
    View publication on PubMed
Search for more literature for 4.6.1.19

Cloned(Commentary)

Cloned (Comment) Organism
expression of GFP-tagged wild-type enzyme and unglycosylated enzyme mutant N37Q/N70Q/N103Q/N123Q in the dolichol pathway-defective alg5DELTA and Golgi-glycosylation-deficient och1DELTA cells and ocalization to the vacuole Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
additional information the DELAT18N mutant lacking the 18 N-terminal amino acids of the signal peptide is catalytically inactive Saccharomyces cerevisiae
N37Q/N70Q/N103Q/N123Q site-directed mutagenesis of N-glycosylation sites, the mutant is mislocated to the vacuole Saccharomyces cerevisiae
W399R site-directed mutagenesis, the mutant is mislocated to the vacuole Saccharomyces cerevisiae

Localization

Localization Comment Organism GeneOntology No. Textmining
endoplasmic reticulum the 18 N-terminal amino acids form the signal peptide responsible for enzyme entry into the endoplasmic reticulum lumen. Enzyme Rny1p requires entering into the endoplasmic reticulum first to become active by N-glycosylation and uses the adaptor protein Erv29p for packaging into COPII vesicles and transport to the Golgi apparatus, wich results in the further attachment of high-glycans Saccharomyces cerevisiae 5783
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extracellular whereas modifications with glycans are dispensable for the nucleolytic activity of Rny1p, Golgi-mediated modifications are critical for its extracellular secretion Saccharomyces cerevisiae
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Golgi apparatus enzyme Rny1p requires entering into the endoplasmic reticulum first to become active by N-glycosylation and uses the adaptor protein Erv29p for packaging into COPII vesicles and transport to the Golgi apparatus, which results in the further attachment of high-glycans. Whereas modifications with glycans are dispensable for the nucleolytic activity of Rny1p, Golgi-mediated modifications are critical for its extracellular secretion. Function of Golgi glycosylation in a T2 RNase as a sorting and secretion signal Saccharomyces cerevisiae 5794
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additional information molecular mechanisms controlling intra- and extracellular localization of enzyme Rny1p , overview. Failure of Golgi-specific glycosylation appears to direct the enzyme to the vacuole as an alternative destination and/or site of terminal degradation, the unglycosylated mutants are unable to be secreted Saccharomyces cerevisiae
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Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
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Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein the enzyme undergoes initial N-linked core glycosylation at four sites, N37, N70, N103 and N123 in the endoplasmic reticulum, four potential N-linked glycosylation sites with the NxS/T consensus sequence in the amino terminal portion of Rny1p: N37KT, N70ET, N103RS and N123DT. The enzyme transport to the Golgi results in the further attachment of high-glycans. Modifications with glycans are dispensable for the nucleolytic enzyme activity. Function of Golgi glycosylation in a T2 RNase as a sorting and secretion signal, overview Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
RNase in Yeast 1
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 Saccharomyces cerevisiae
Rny1p
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 Saccharomyces cerevisiae
T2 RNase
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 Saccharomyces cerevisiae

General Information

General Information Comment Organism
evolution the enzyme belongs to the the T2 family of RNases Saccharomyces cerevisiae
malfunction GFP-tagged enzyme wild-type and mutants N37Q/N70Q/N103Q/N123Q and W399R localize to the vacuole, the unglycosylated mutants are unable to be secreted, overview. Glycosylation-defective Rny1p mutants are not destroyed via the ERAD mechanism Saccharomyces cerevisiae
additional information enzyme Rny1p requires entering into the endoplasmic reticulum first to become active and uses the adaptor protein Erv29p for packaging into COPII vesicles and transport to the Golgi apparatus Saccharomyces cerevisiae