Genetic studies in budding yeast have previously implicated SLX5 and SLX8 in the control of genome stability and sumoylation. These genes encode RING-finger domain proteins that form a complex of unknown function. Because RING-finger proteins comprise a large class of ubiquitin (Ub) ligases, Slx5 and Slx8 were tested for this activity. Here we show that the Slx5-Slx8 complex, but not its individual subunits, stimulates several human and yeast Ub conjugating enzymes, including Ubc1, 4, 5, and Ubc13-Mms2. The RING-finger domains of both subunits are genetically required for suppression of slx sgs1Delta synthetic-lethality, and point mutations that abolish Ub ligase activity in vitro also eliminate in vivo complementation. Targets of the in vitro ubiquitination reaction include the Slx5 and Slx8 subunits themselves, and the homologous recombination proteins Rad52 and Rad57. We propose that the Slx5-Slx8 complex functions as a two-component Ub ligase in vivo and that it controls genome stability and sumoylation via ubiquitination.
Increase the total number of rows showing on this page using the pull-down located below the table, or use the page scroll at the table's top right to browse through the table's pages; use the arrows to the right of a column header to sort by that column; filter the table using the "Filter" box at the top of the table.
Gene/Complex | Qualifier | Gene Ontology Term | Annotation Extension | Evidence | Source | Assigned On |
---|---|---|---|---|---|---|
Slx5-Slx8 SUMO-targeted ubiquitin ligase (STUbL) complex | enables | ubiquitin-protein transferase activity | IDA | ComplexPortal | 2014-10-16 | |
SLX5 | contributes to | ubiquitin-protein transferase activity | has input RAD57 | IDA | SGD | 2019-11-06 |
SLX5 | contributes to | ubiquitin-protein transferase activity | has input RAD52 | IDA | SGD | 2019-11-06 |
SLX8 | involved in | protein ubiquitination | IDA | SGD | 2013-08-07 | |
SLX8 | contributes to | ubiquitin-protein transferase activity | has input RAD57 | IDA | SGD | 2019-11-06 |
SLX8 | contributes to | ubiquitin-protein transferase activity | has input RAD52 | IDA | SGD | 2019-11-06 |
Increase the total number of rows showing on this page using the pull-down located below the table, or use the page scroll at the table's top right to browse through the table's pages; use the arrows to the right of a column header to sort by that column; filter the table using the "Filter" box at the top of the table; click on the small "i" buttons located within a cell for an annotation to view further details.
Gene | Phenotype | Experiment Type | Mutant Information | Strain Background | Chemical | Details |
---|---|---|---|---|---|---|
SLX5 | resistance to chemicals: decreased | classical genetics | null Allele: slx5-Δ | W303 | hydroxyurea | |
SLX8 | resistance to chemicals: decreased | classical genetics | null Allele: slx8-Δ | W303 | hydroxyurea | |
SLX5 | resistance to chemicals: decreased | classical genetics | reduction of function Allele: slx5-6 C494A,C497A mutations in RING domain | W303 | hydroxyurea | |
SLX5 | resistance to chemicals: decreased | classical genetics | reduction of function Allele: slx5-8 C556S,H558A,C561S mutations in RING domain | W303 | hydroxyurea | |
SLX5 | resistance to chemicals: decreased | classical genetics | reduction of function Allele: slx5-9 deletion of RING domain | W303 | hydroxyurea | |
SLX8 | resistance to chemicals: decreased | classical genetics | reduction of function Allele: slx8-6 deletion of RING domain | W303 | hydroxyurea | |
SLX8 | resistance to chemicals: decreased | classical genetics | reduction of function Allele: slx8-3 C221S,H223A,C226S mutations in RING domain | W303 | hydroxyurea | |
SLX8 | resistance to chemicals: decreased | classical genetics | reduction of function Allele: slx8-1 C221Y mutation in RING domain | W303 | hydroxyurea |
Increase the total number of rows showing on this page by using the pull-down located below the table, or use the page scroll at the table's top right to browse through the table's pages; use the arrows to the right of a column header to sort by that column; filter the table using the "Filter" box at the top of the table; click on the small "i" buttons located within a cell for an annotation to view further details about experiment type and any other genes involved in the interaction.
Evidence ID | Analyze ID | Interactor | Interactor Systematic Name | Interactor | Interactor Systematic Name | Allele | Assay | Annotation | Action | Phenotype | SGA score | P-value | Source | Reference | Note |
---|
Increase the total number of rows showing on this page by using the pull-down located below the table, or use the page scroll at the table's top right to browse through the table's pages; use the arrows to the right of a column header to sort by that column; filter the table using the "Filter" box at the top of the table; click on the small "i" buttons located within a cell for an annotation to view further details about experiment type and any other genes involved in the interaction.
Interactor | Interactor | Assay | Annotation | Action | Modification | |
---|---|---|---|---|---|---|
the slx5-slx8 complex can form ubiquitin chains in vitro | SLX5 | UBI4 | Biochemical Activity | manually curated | Bait-Hit | ubiquitinylated lysine |
the slx5-slx8 complex can form ubiquitin chains in vitro | SLX8 | UBI4 | Biochemical Activity | manually curated | Bait-Hit | ubiquitinylated lysine |
SLX8 | SLX5 | Reconstituted Complex | manually curated | Bait-Hit | No Modification |