3.4.22.B67: Ulp2 peptidase
This is an abbreviated version!
For detailed information about Ulp2 peptidase, go to the full flat file.
Word Map on EC 3.4.22.B67
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3.4.22.B67
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sumoylation
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checkpoint
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deconjugation
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sumo-1
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sumo-protein
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helicase
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sumo-specific
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hydroxyurea
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restart
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nuclear-localization
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poly-sumo
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dna-damaging
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nucleolar
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ubiquitin-related
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spindle
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euploidy
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polysumoylation
- 3.4.22.B67
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sumoylation
-
checkpoint
-
deconjugation
- sumo-1
-
sumo-protein
- helicase
-
sumo-specific
- hydroxyurea
-
restart
-
nuclear-localization
-
poly-sumo
-
dna-damaging
-
nucleolar
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ubiquitin-related
-
spindle
-
euploidy
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polysumoylation
Reaction
Ulp2 hydrolyses the SUMO-SUMO linkage in poly-SUMO chains. It catalyzes desumoylation of SUMO-modified-Ndc10 kinetochore protein, SUMO-modified-Bir1 kinetochore protein or SUMO-modified-Cep3 kinetochore protein. =
Synonyms
At1g09730, at4g33620, probable ubiquitin-like-specific protease 2A, probable ubiquitin-like-specific protease 2B, Smt3-specific protease, SMT4, Spf1, SPF2, SUMO de-conjugating/chain-editing enzyme Ulp2p, SUMO isopeptidase Ulp2, SUMO protease, SUMO(Smt3)-specific protease, SUMO-specific protease, Ulp2, ULP2 SUMO isopeptidase, Ulp2 SUMO protease, Ulp2A, Ulp2B, Ulp2p
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General Information
General Information on EC 3.4.22.B67 - Ulp2 peptidase
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malfunction
physiological function
deletion of ULP2 promotes the accumulation of poly-SUMO chains and suppresses sgs1DELRA slx5D synthetic lethality and the slx5DELTA sporulation defect. It is speculated that the loss of ULP2 suppresses the toxicity of the sumoylated proteins that accumulate in slx5D-slx8D cells by permitting the extension of poly-SUMO chains on specific target proteins
malfunction
deletion of ULP2 results in a diverse set of aberrations, but the gene is not essential. In cells lacking Ulp2, specific Smt3-protein conjugates accumulate, and the conjugate pattern is distinct from that observed in a ulp1ts strain, which is defective for a distantly related Smt3-specific protease, Ulp1. The ulp2D mutant exhibits a pleiotropic phenotype that includes temperature-sensitive growth, abnormal cell morphology, decreased plasmid and chromosome stability, and a severe sporulation defect. The mutant is also hypersensitive to DNA damaging agents, hydroxyurea, and benomyl
malfunction
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disruption of Ulp2 causes a range of phenotypic defects, including temperature sensitivity, chromosome instability, and hypersensitivity to DNA and spindle damage. Ulp2-deleted cells died in the presence of DNA damage. In the presence of a DNA double-strand break, ulp2DELTA cells permanently arrested as large-budded cells regardless of whether the DNA DNA double-strand break is repairable or not
malfunction
in yeast, mutants lacking Ulp2 accumulate high molecular weight SUMO-containing species only in the presence of wild-type Smt3. This is not the case in the smt3 mutants that do not have the critical lysine residues. Ulp2DELTA mutant strains are impaired in the mitotic-specific targeting of the condensin complex to chromatin, in particular rDNA chromatin. In addition, Ulp2 mutants display an increase in premature separation and fail to maintain cohesion at the regions proximal to centromere, which is caused in part by the poor regulation of the SUMO modification status of DNA Topoisomerase II
malfunction
inactivation of ULP2 in a strain expressing wild-type SUMO-activating enzyme results in slow and temperature-sensitive growth, and accumulation of SUMO conjugates
malfunction
spontaneous recombination is elevated in ulp2 strains. Ulp2 mutants display a reduced frequency of chromosome rearrangements. ulp2D mutants fail in chromosome segregation after exposure to methyl methanesulfonate
malfunction
ulp2DELTA mutants do not show persistent Rad53 phosphorylation following DNA damage, suggesting checkpoint signaling has been terminated and no longer asserts an arrest in these cells. Using Cdc14 localization as a cell cycle indicator, it is shown that nearly half of cells lacking Ulp2 can escape a checkpoint-induced metaphase arrest despite their inability to divide again. Moreover, half of permanently arrested ulp2DELTA cells show evidence of an aberrant mitotic spindle, suggesting that Ulp2 is required for proper spindle dynamics during cell cycle resumption following a DNA damage-induced cell cycle arrest
malfunction
a robust SUMO stress response occurs in response to 1 M sorbitol treatment of a ulp2 deletant strain
malfunction
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a robust SUMO stress response occurs in response to 1 M sorbitol treatment of a ulp2 deletant strain
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role for Ulp2p in preventing the formation of DNA lesions that must be repaired through recombination. Ulp2p is also required to either suppress or resolve recombination-induced attachments between sister chromatids
physiological function
Ulp2 is a nuclear protein required for chromosome stability and cell cycle restart after checkpoint arrest
physiological function
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Ulp2 is required for cell division following termination of the DNA damage checkpoint in Sacharomyces cerevisiae. The DNA damage checkpoint is a crucial defense mechanism used by cells to withstand DNA damage. Activation of the checkpoint halts the cell cycle at metaphase and allows time for DNA repair prior to cell division. Potentially, Ulp2 might be a part of the recovery and adaptation mechanisms but might act at a very late step to turn off the DNA damage-signaling cascade. An alternative, but not mutually exclusive, possibility is that Ulp2 acts after turnoff of the damage-signaling cascade to promote a step in cell division following release from the metaphase arrest. In either case, the role of Ulp2 most likely involves the desumoylation of one or more protein substrates, as we found that the SUMO protease activity of Ulp2 is required for its function and that inhibiting protein-SUMO conjugation could suppress the permanent arrest of ulp2DELTA cells after DNA damage
physiological function
Ulp2 is required for proper spindle dynamics during cell cycle resumption following a DNA damage-induced cell cycle arrest
physiological function
Ulp2 is required for the maintenance of chromosome structures. Ulp2 is specialized for chain editing activities
physiological function
Ulp2 prevents accumulation of SUMO chains in yeast
physiological function
isozyme Ulp2 controls the dynamic range of small ubiquitin-related modifiers, SUMO, chain lengths by trimming them from the distal ends
physiological function
the enzyme inhibits SUMO stress response consisting of consist of a simple SUMO conjugation-deconjugation cycle, overview. Isozyme Ulp2 is required to prevent the accumulation of SUMO chains in budding yeast
physiological function
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cells lacking Ulp2 display a twofold increase in transcript levels across chromosome I (ChrI) and ChrXII. This is due to the two chromosomes being present at twice their normal copy number. Extra copies of ChrI and ChrXII appear quickly following loss of active Ulp2 and can be eliminated following reintroduction of Ulp2 gene. Increased dosage of two genes on ChrI-CLN3 and CCR4, encoding a G1-phase cyclin and a subunit of the Ccr4-Not deadenylase complex, respectively, suppresses Ulp2-dependent aneuploidy
physiological function
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loss of Upl2 results in ChrI disomy, which is eliminated by extended passaging. The mRNA levels for almost all ribosomal proteins increase transiently upon initial loss of Ulp2, but elevated Ccr4 deadenylase levels limit excess ribosome formation. Extended passaging leads to increased levels of many small nucleolar RNAs involved in ribosome biogenesis, and higher dosage of three linked ChrXII small nucleolar RNA genes suppress ChrXII disomy in Ulp2 mutant cells
physiological function
loss-of-function mutant's phenotypes included late flowering, altered leaf morphology and severely impaired seed production. Seeds are also bigger. Mutants constitutively accumulate SUMO conjugates, and expression in yeast complements the loss of Ulp2 but not ScUlp1. Isoform Spf1 seems to be much more expressed than isoform Spf2. Compared to Spf2, Spf1 mutant alleles display more prominent phenotypes in leaf morphology, flowering time, pigment accumulation, and increased SUMO conjugates
physiological function
the C-terminal regulatory domain of Ulp2 contains three distinct conserved motifs that control its in vivo substrate specificity and cell growth. Among them, a SUMO-interacting motif (SIM) coordinates with the domain of Ulp2 that binds to the nucleolar protein Csm1 to ensure maximal deSUMOylation of Ulp2's nucleolar substrates. The Csm1-binding domain of Ulp2 recruits this enzyme to the nucleolus, and Ulp2's C-terminal SIM promotes its SUMO protease activity and plays a key role in mediating the in vivo specificity of Ulp2
physiological function
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Ulp2 is recruited to transcriptionally active genes to control local polysumoylation. Mutant Ulp2 cells show impaired association of RNA polymerase II with, and diminished expression of, constitutively active genes and the inducible CUP1 gene. Ulp2 loss sensitizes cells to 6-azauracil, a hallmark of transcriptional elongation defects
physiological function
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the enzyme inhibits SUMO stress response consisting of consist of a simple SUMO conjugation-deconjugation cycle, overview. Isozyme Ulp2 is required to prevent the accumulation of SUMO chains in budding yeast
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