<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Kumar B</submitter><funding>NIDDK NIH HHS</funding><pagination>39523-35</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC2998155</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>285(50)</volume><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</pubmed_abstract><journal>The Journal of biological chemistry</journal><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.</pubmed_title><pmcid>PMC2998155</pmcid><funding_grant_id>R01 DK46181</funding_grant_id><funding_grant_id>R01 DK046181</funding_grant_id><pubmed_authors>DeMartino GN</pubmed_authors><pubmed_authors>Kumar B</pubmed_authors><pubmed_authors>Kim YC</pubmed_authors></additional><is_claimable>false</is_claimable><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.</name><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</description><dates><release>2010-01-01T00:00:00Z</release><publication>2010 Dec</publication><modification>2025-04-04T20:12:59.605Z</modification><creation>2019-03-27T00:37:13Z</creation></dates><accession>S-EPMC2998155</accession><cross_references><pubmed>20937828</pubmed><doi>10.1074/jbc.m110.153627</doi><doi>10.1074/jbc.M110.153627</doi></cross_references></HashMap>