Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Cell cycle mechanisms of sister chromatid separation; roles of Cut1/separin and Cut2/securin.
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Securin (Cut2) is an APC/cyclosome target that is polyubiquitinated in a destruction-box-dependent manner before destruction.
"Securin, like mitotic cyclins, is the target of the anaphase promoting complex (APC)/cyclosome and is polyubiquitinated before destruction in a manner dependent upon the destruction sequence."
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Anaphase does not occur properly without securin destruction.
"The anaphase never occurs properly in the absence of securin destruction."
Proteomics analysis identifies new components of the fission and budding yeast anaphase-promoting complexes.
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TAP purification with direct mass-spectrometric analysis (DALPC) of the S. pombe and S. cerevisiae APC/C identified 13 subunits in each yeast, including small subunits such as apc11 that earlier approaches had missed.
"Our data increase the total number of identified APC subunits to 13 in both yeasts and indicate that previous approaches were biased against the identification of small subunits."
Swm1/Apc13 is an evolutionarily conserved subunit of the anaphase-promoting complex stabilizing the association of Cdc16 and Cdc27.
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Apc11 carries the RING finger of the APC/C and has minimal ubiquitin ligase properties on its own.
"APC/C's RING finger is located within the small subunit Apc11, which by itself has the properties of a minimal ubiquitin ligase ( 13 , 22 )."
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Apc11 is anchored to the complex through the cullin-related subunit Apc2.
"Apc11 is anchored to the complex through Apc2, a subunit distantly related to cullins ( 50 , 54 )."
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TAP-tagged Cut9 and Apc13 purified from fission yeast recover the full set of known and predicted APC/C subunits.
"Accordingly, purification of a TAP-tagged version of Apc13 yielded the same set of APC/C subunits as Cut9-TAP (Fig. 2C ), demonstrating that apc13 + encodes a subunit of the fission yeast APC/C."
The APC11 RING-H2 finger mediates E2-dependent ubiquitination.
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Budding-yeast Apc11 alone defines the minimal ubiquitin ligase activity of the APC/C.
"Here, we provide evidence that the Saccharomyces cerevisiae RING-H2 finger protein Apc11 defines the minimal ubiquitin ligase activity of the APC."
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Purified Apc11 binds the E2 Ubc4 directly.
"Using purified, recombinant proteins we showed that Apc11p interacted directly with the Ubc4 ubiquitin conjugating enzyme (E2)."
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Apc11 polyubiquitinates the cyclin Clb2 in vitro with Ubc4, and the RING-H2 finger is absolutely required for this E3 activity.
"However, Apc11p bearing mutations in putative metal-binding cysteines (C41, C44, or C91) showed little or no activity in this assay (Figure 5 A, lanes 3, 4, and 9), demonstrating that the RING-H2 finger is absolutely required for its E3 activity."
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RING-based E3s act as bridges between E2 and substrate rather than forming thioester intermediates.
"Our work, and that of others, indicates that RING-based E3s do not act as ubiquitin carriers that form thioester intermediates, but instead act as bridges between E2s and substrates that provide a favorable environment for the transfer of ubiquitin."
APC2 Cullin protein and APC11 RING protein comprise the minimal ubiquitin ligase module of the anaphase-promoting complex.
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The APC2-APC11 heterodimer with Ubc4 or UbcH10 suffices to ubiquitinate securin and cyclin B1.
"In combination with Ubc4 or UbcH10, a heterodimeric complex of APC2 and APC11 is sufficient to catalyze the ubiquitination of human securin and cyclin B1."
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The minimal APC2/11 module lacks substrate specificity.
"However, the minimal APC2/11 ubiquitin ligase module does not possess substrate specificity, because it also ubiquitinates the destruction box deletion mutants of securin and cyclin B1."
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APC11 binds the C-terminal cullin homology domain of APC2, and Ubc4 binds APC11 directly.
"Both APC11 and UbcH10 bind to the C-terminal cullin homology domain of APC2, whereas Ubc4 interacts with APC11 directly."
Cut2 proteolysis required for sister-chromatid seperation in fission yeast.
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Cut2/securin is nuclear and spindle-associated, is degraded at anaphase by the Cut9-containing APC/cyclosome, and its regulated proteolysis is essential for sister-chromatid separation.
"The rapid degradation of Cut2 at anaphase requires its amino-terminal region and the activity of Cut9 (ref. 14), a component of the 20S cyclosome/anaphase-promoting complex (APC), which is necessary for cyclin destruction."
The spindle checkpoint functions of Mad3 and Mad2 depend on a Mad3 KEN box-mediated interaction with Cdc20-anaphase-promoting complex (APC/C).
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The APC/C is the E3 that labels securin and cyclins for destruction.
"Mitotic progression is driven by proteolytic destruction of securin and cyclins. These proteins are labeled for destruction by an ubiquitin-protein isopeptide ligase (E3) known as the anaphase-promoting complex or cyclosome (APC/C)."
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The APC/C requires Cdc20/Slp1 or Cdh1 activators to recognise D-box and KEN-box substrates.
"The APC/C requires activators (Cdc20 or Cdh1) to efficiently recognize its substrates, which are specified by destruction (D box) and/or KEN box signals."
Role of Hcn1 and its phosphorylation in fission yeast anaphase-promoting complex/cyclosome function.
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The S. pombe APC/C becomes active at the metaphase/anaphase transition and remains active during G1.
"The APC/C becomes active at the metaphase/anaphase transition and remains active during G(1) phase."
Analysis of a genome-wide set of gene deletions in the fission yeast Schizosaccharomyces pombe.
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Systematic deletion analysis determined the essentiality of 4,836 fission yeast genes; PomBase records the apc11 deletion as inviable (FYPO:0002061) on this basis.
"We determined the essentiality of 4,836 genes by sporulating each heterozygous deletion diploid strain followed by microscopic observation of the germinating haploid spores."
Mps1Mph1 Kinase Phosphorylates Mad3 to Inhibit Cdc20Slp1-APC/C and Maintain Spindle Checkpoint Arrests.
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Reconstituted S. pombe APC/C ubiquitination of Cut2 uses fission-yeast E1 (Uba1) and the E2s Ubc1, Ubc4 and Ubc11 together with Slp1.
"In brief, 0.05 mg/ml Uba1, 0.5mg/ml E2s (ubc1, ubc4 and ubc11) and 0.3 mM ATP were mixed with 1.5 mg/ml wild-type mono-ubiquitin (Sigma Aldrich), 2μM ubiquitin aldehyde (Boston Biochem) in a ubiquitination buffer containing 25 mM HEPES pH 7.5, 100 mM KCl, 3mM ATP, 2.5 mM MgCl2, and 0.2 mM DTT."
Falcon (Edison) deep research report for S. pombe apc11
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Purified mitotic S. pombe APC/C ubiquitylates a Cdc2-Cdc13 substrate in an E1-, E2- and ATP-dependent assay, and cellular APC/C activity generates ubiquitylated Cut2.
"APC/C ubiquitylated a Cdc2–Cdc13 substrate in an E1-, E2-, and ATP-dependent assay, while cellular APC/C activity generated ubiquitylated Cut2."
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Apc11 is present at one copy per APC/C particle and occupies the catalytic side of the complex with Apc2 and Apc10 (Ohi et al. 2007, not cached).
"Apc11, Apc2, and Apc10 occupy the catalytic side of the assembly, spatially separated from much of the TPR scaffold."
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Fission-yeast APC/C uses Ubc11 for initial substrate modification and Ubc4 for chain extension.
"Ubc11 can generate short ubiquitin chains in the absence of Ubc4, whereas Ubc4 cannot ubiquitylate APC/C substrates without Ubc11, supporting a model in which Ubc11 participates in initial substrate modification and Ubc4 supports chain extension."
UniProt entry Q9UT86 (APC11_SCHPO)
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UniProt lists apc11 among the 13 subunits of the S. pombe APC/C based on Yoon et al. 2002.
"The APC/C is composed of at least 13 subunits: apc1, apc2,"