EC Number   |
General Information |
Reference |
|---|
   5.6.1.5 | evolution |
the enzyme contains an AAA ATPase domain, phylogenetic analysis |
-, 755713 |
| 5.6.1.5 | malfunction |
destabilization of the N-terminal coiled-coil regions of Rpt subunits causes proteasome defects, destabilization of Rpt subunits hampers yeast growth |
735031 |
| 5.6.1.5 | malfunction |
disruption of nucleotide binding to an Rpt subunit by mutation in the Walker A motif inhibits the assembly of the Rpt ring without affecting heterodimer formation with its partner Rpt subunit. Coexpression of the base assembly chaperones S5b and PAAF1 with mutant Rpt1 and Rpt6, respectively, relieves assembly inhibition of mutant Rpts by facilitating their interaction with adjacent Rpt dimers. The mutation in the Walker B motif which impairs ATP hydrolysis does not affect Rpt ring formation. Incorporation of a Walker B mutant Rpt subunit abrogates the ATPase activity of the 19S RP, suggesting that failure of the mutant Rpt to undergo the conformational transition from an ATP-bound to an ADP-bound state impairs conformational changes in the other five wild-type Rpts in the Rpt ring. Deletion of the HbYX motif impairs the efficient assembly of the ATPase ring in the 19S RP, whereas C-terminal deletions in Rpts not possessing the HbYX motif do not have any deleterious effect on proteasome assembly |
734207 |
| 5.6.1.5 | malfunction |
in cells deficient for AAA-ATPases of the proteasome 19S regulatory particle, the cholesterol biosynthetic enzyme 3-hydroxy-3-methylglutaryl-coenzyme A reductase continued to become membrane-extracted, but not cytosolically dislocated |
734264 |
| 5.6.1.5 | malfunction |
loss of Rpt6's partially unfolded state by glycine substitution in Rpt6 mutant G360A/G387A disrupts holoenzyme formation in vitro, an effect enhanced by Rpn14. Loss of Rpt6 conformational exchange enhances Rpn14 requirement during proteasome stress. Saccharomyces cerevisiae lacking Rpn14 and with Rpt6 mutant G360A/G387A incorporated demonstrate hallmarks of defective proteasome assembly and synthetic growth defects |
735289 |
| 5.6.1.5 | malfunction |
RPT2a is an upstream signaling component for inducing both defense and morphological phenotypes in the uni-1D mutant. Loss of function of RPT2a suppresses the uni-1D-induced phenotypes caused by the activated cytokinin signaling |
720657 |
| 5.6.1.5 | malfunction |
subunit PSMC5 depletion in H-460 cells enhances both AKT activation and MDM2 transcription, thereby promoting the degradation of p53 and p21 proteins |
749804 |
| 5.6.1.5 | metabolism |
the ATPase motor of the 26S proteasome unfolds and translocates targeted protein substrates into the open gate of a proteolytic core while a proteasomal deubiquitinase concomitantly removes substrate-attached ubiquitin chains |
752260 |
| 5.6.1.5 | metabolism |
the enzyme captures, unfolds, and translocates protein substrates into the 20S proteasome core particle for degradation |
751584 |
| 5.6.1.5 | metabolism |
the enzyme complex binds and regulates the eukaroytic 26S proteasome |
751651 |
