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Literature summary for 3.4.22.68 extracted from

  • Elmore, Z.C.; Donaher, M.; Matson, B.C.; Murphy, H.; Westerbeck, J.W.; Kerscher, O.
    Sumo-dependent substrate targeting of the SUMO protease Ulp1 (2011), BMC Biol., 9, 74.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.22.68

Application

Application Comment Organism
biotechnology substrate-trapping Ulp1(3)(C580S) interacts robustly with human SUMO1, SUMO2 and SUMO2 chains, making it a potentially useful tool for the analysis and purification of SUMO-modified proteins Saccharomyces cerevisiae
molecular biology usage of the targeting and small ubiquitin-like modifier, SUMO, binding properties of Ulp1(3)(C580S) to purify Smt3-modified proteins from cell extracts Saccharomyces cerevisiae

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant enzymes, expression of the SBS domain as a SBS-GFP fusion protein Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
C580S site-directed mutagenesis, generation of a catalytically inactive mutant of Ulp1, the mutant is greatly enriched at the septin ring of dividing yeast cells. The 218-amino acid, substrate-trapping mutant of the catalytic domain of Ulp1 is necessary and sufficient for septin localization Saccharomyces cerevisiae
D451N the mutation destroys an essential salt bridge formed between Smt3 and Ulp1 Saccharomyces cerevisiae
D451N/C580S site-directed mutagenesis, abolished accumulation of the full-length Ulp1 double-mutant at the septin ring Saccharomyces cerevisiae
I435V/N450S/I504T/C580S site-directed mutagenesis, the mutant shows a reduced ability to enrich at the septin ring Saccharomyces cerevisiae
additional information generation of a collection of GFP-tagged Ulp1 truncations and domains that were expressed under control of the Ulp1 promoter. truncations and domains of Ulp1, that retain substrate targeting information, also localize to the septin ring in G2/M-arrested cells. Usage of the targeting and SUMO-binding properties of Ulp1(3)(C580S) to purify Smt3-modified proteins from cell extracts. Deletion of the entire SBS domain on the localization of Ulp1(3)(C580S). The Ulp1(3)(C580S)SBSDELTA construct does not localize to the septin ring in the majority of cells Saccharomyces cerevisiae

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm Ulp1 localizes predominantly to nuclear pore complexes but also deconjugates sumoylated septins at the bud-neck of dividing cells. A 218-amino acid, substrate-trapping mutant of the catalytic domain of Ulp1, Ulp1(3) C580S is necessary and sufficient for septin localization Saccharomyces cerevisiae 5737
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nuclear pore complex Ulp1 localizes predominantly to nuclear pore complexes but also deconjugates sumoylated septins at the bud-neck of dividing cells Saccharomyces cerevisiae
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Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information Ulp1 is responsible for both removing SUMO/Smt3 from specific target proteins and for processing precursor SUMO into its conjugation-competent form. Multiple features in the catalytic domain of Ulp1 affect SUMO interactions, analysis of features of Ulp1 required for substrate targeting, structure-function analysis, overview. D451 is required for targeting of sumoylated proteins and the C580S mutation is required for retention of Ulp1 at the septin ring. Kap121-independent SUMO-targeting information resides in the catalytic domain of Ulp1. The Ulp1 Kap121-interacting domain (region 1), the Ulp1 Kap60/Kap95-interacting domain (region 2) and the catalytic domain (region 3) fail to interact with the Smt3-binding domain Saccharomyces cerevisiae ?
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Synonyms

Synonyms Comment Organism
SUMO protease
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 Saccharomyces cerevisiae
Ulp1
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 Saccharomyces cerevisiae
Ulp1 protease
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 Saccharomyces cerevisiae

General Information

General Information Comment Organism
physiological function Ulp1 facilitates sumoylation by processing precursor SUMO into its conjugation competent form. Conversely, Ulp1 also facilitates desumoylation by removing SUMO from nuclear and cytosolic proteins after conjugation. The essential small ubiquitin-like modifier, SUMO, protease Ulp1 is responsible for both removing SUMO/Smt3 from specific target proteins and for processing precursor SUMO into its conjugation-competent form Saccharomyces cerevisiae