{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Kumar B"],"funding":["NIDDK NIH HHS"],"pagination":["39523-35"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC2998155"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["285(50)"],"pubmed_abstract":["PA700, the 19 S regulatory subcomplex of the 26 S proteasome, contains a heterohexameric ring of AAA subunits (Rpt1 to -6) that forms the binding interface with a heteroheptameric ring of α subunits (α1 to -7) of the 20 S proteasome. Binding of these subcomplexes is mediated by interactions of C termini of certain Rpt subunits with cognate binding sites on the 20 S proteasome. Binding of two Rpt subunits (Rpt2 and Rpt5) depends on their last three residues, which share an HbYX motif (where Hb is a hydrophobic amino acid) and open substrate access gates in the center of the α ring. The relative roles of other Rpt subunits for proteasome binding and activation remain poorly understood. Here we demonstrate that the C-terminal HbYX motif of Rpt3 binds to the 20 S proteasome but does not promot"],"journal":["The Journal of biological chemistry"],"pubmed_title":["The C terminus of Rpt3, an ATPase subunit of PA700 (19 S) regulatory complex, is essential for 26 S proteasome assembly but not for activation."],"pmcid":["PMC2998155"],"funding_grant_id":["R01 DK46181","R01 DK046181"],"pubmed_authors":["DeMartino GN","Kumar B","Kim YC"],"additional_accession":[]},"is_claimable":false,"name":"The C terminus of Rpt3, an ATPase subunit of PA700 (19 S) regulatory complex, is essential for 26 S proteasome assembly but not for activation.","description":"PA700, the 19 S regulatory subcomplex of the 26 S proteasome, contains a heterohexameric ring of AAA subunits (Rpt1 to -6) that forms the binding interface with a heteroheptameric ring of α subunits (α1 to -7) of the 20 S proteasome. Binding of these subcomplexes is mediated by interactions of C termini of certain Rpt subunits with cognate binding sites on the 20 S proteasome. Binding of two Rpt subunits (Rpt2 and Rpt5) depends on their last three residues, which share an HbYX motif (where Hb is a hydrophobic amino acid) and open substrate access gates in the center of the α ring. The relative roles of other Rpt subunits for proteasome binding and activation remain poorly understood. Here we demonstrate that the C-terminal HbYX motif of Rpt3 binds to the 20 S proteasome but does not promot","dates":{"release":"2010-01-01T00:00:00Z","publication":"2010 Dec","modification":"2025-04-04T20:12:59.605Z","creation":"2019-03-27T00:37:13Z"},"accession":"S-EPMC2998155","cross_references":{"pubmed":["20937828"],"doi":["10.1074/jbc.m110.153627","10.1074/jbc.M110.153627"]}}