Genomes and Genes
Gene Symbol: RPT4
Description: proteasome regulatory particle base subunit RPT4
Alias: CRL13, PCS1, SUG2, proteasome regulatory particle base subunit RPT4
Species: Saccharomyces cerevisiae S288c
- Park S, Roelofs J, Kim W, Robert J, Schmidt M, Gygi S, et al. Hexameric assembly of the proteasomal ATPases is templated through their C termini. Nature. 2009;459:866-70 pubmed publisher..The Rpt proteins with the strongest assembly phenotypes, Rpt4 and Rpt6, were absent from BP1...
- Matyskiela M, Lander G, Martin A. Conformational switching of the 26S proteasome enables substrate degradation. Nat Struct Mol Biol. 2013;20:781-8 pubmed publisher..Notably, Rpn11 moves from an occluded position to directly above the central pore, thus facilitating substrate deubiquitination concomitant with translocation. ..
- Lipson C, Alalouf G, Bajorek M, Rabinovich E, Atir Lande A, Glickman M, et al. A proteasomal ATPase contributes to dislocation of endoplasmic reticulum-associated degradation (ERAD) substrates. J Biol Chem. 2008;283:7166-75 pubmed publisher..Together, we find that equivalent mutations in RPT4 and RPT2 result in different phenotypes...
- Lander G, Estrin E, Matyskiela M, Bashore C, Nogales E, Martin A. Complete subunit architecture of the proteasome regulatory particle. Nature. 2012;482:186-91 pubmed publisher..We provide a structural basis for the ability of the proteasome to degrade a diverse set of substrates and thus regulate vital cellular processes. ..
- Li S, Spooner R, Allen S, Guise C, Ladds G, Schnöder T, et al. Folding-competent and folding-defective forms of ricin A chain have different fates after retrotranslocation from the endoplasmic reticulum. Mol Biol Cell. 2010;21:2543-54 pubmed publisher..We conclude that cytosolic ERAD components, particularly the proteasome RP, can discriminate between structural features of the same substrate. ..
- Malik S, Shukla A, Sen P, Bhaumik S. The 19 s proteasome subcomplex establishes a specific protein interaction network at the promoter for stimulated transcriptional initiation in vivo. J Biol Chem. 2009;284:35714-24 pubmed publisher..Together, these results provide significant insights as to how the 19 S proteasome subcomplex regulates the formation of the active transcription complex assembly (and, hence, transcriptional initiation) at the promoter in vivo. ..
- Takeuchi J, Tamura T. Recombinant ATPases of the yeast 26S proteasome activate protein degradation by the 20S proteasome. FEBS Lett. 2004;565:39-42 pubmed..Purification of the Rpt1Rpt2 hetero-complex and the Rpt4 homo-complex for functional characterization demonstrated their contribution to energy-dependent protein ..
- Geng F, Tansey W. Similar temporal and spatial recruitment of native 19S and 20S proteasome subunits to transcriptionally active chromatin. Proc Natl Acad Sci U S A. 2012;109:6060-5 pubmed publisher..We find that proteasome subunits Rpt1, Rpt4, Rpn8, Rpn12, Pre6, and Pre10 are recruited to GAL10 rapidly upon galactose induction...
- Xie Y, Varshavsky A. UFD4 lacking the proteasome-binding region catalyses ubiquitination but is impaired in proteolysis. Nat Cell Biol. 2002;4:1003-7 pubmed..Here we advance this analysis for UFD4 and show that it interacts with RPT4 and RPT6, two subunits of the 19S particle...
- Sulahian R, Sikder D, Johnston S, Kodadek T. The proteasomal ATPase complex is required for stress-induced transcription in yeast. Nucleic Acids Res. 2006;34:1351-7 pubmedSug1 and Sug2 are two of six ATPases in the 19S regulatory particle of the 26S proteasome. We have shown previously that these proteins play a non-proteolytic role in the transcription of the GAL genes in yeast...
- Sun L, Johnston S, Kodadek T. Physical association of the APIS complex and general transcription factors. Biochem Biophys Res Commun. 2002;296:991-9 pubmed..These data add to the growing body of evidence that the APIS complex has a role in transcription, independent of its role in proteolysis and, furthermore, argues that it functions in association with the general transcription complex. ..
- Kingsbury J, McCusker J. Homoserine toxicity in Saccharomyces cerevisiae and Candida albicans homoserine kinase (thr1Delta) mutants. Eukaryot Cell. 2010;9:717-28 pubmed publisher..Since the doa4Delta and proteasome mutants identified have reduced ubiquitin- and/or proteasome-mediated proteolysis, the degradation of a particular protein or subset of proteins likely contributes to homoserine toxicity...
- Gillette T, Huang W, Russell S, Reed S, Johnston S, Friedberg E. The 19S complex of the proteasome regulates nucleotide excision repair in yeast. Genes Dev. 2001;15:1528-39 pubmed..The 19S regulatory complex of the yeast proteasome functions in nucleotide excision repair independent of proteolysis. ..
- McDonald H, Helfant A, Mahony E, Khosla S, Goetsch L. Mutational analysis reveals a role for the C terminus of the proteasome subunit Rpt4p in spindle pole body duplication in Saccharomyces cerevisiae. Genetics. 2002;162:705-20 pubmed..Previously, we reported that a conditional mutation in the Saccharomyces cerevisiae gene RPT4/PCS1, which encodes one of six ATPases in the proteasome 19S cap complex/regulatory particle (RP), causes failure of ..
- Russell S, Gonzalez F, Joshua Tor L, Johnston S. Selective chemical inactivation of AAA proteins reveals distinct functions of proteasomal ATPases. Chem Biol. 2001;8:941-50 pubmed..Mutation of a threonine in the active site of Sug1/Rpt6 or Sug2/Rpt4 to a cysteine sensitizes these proteins to inactivation through alkylation by the sulfhydryl modifying agent ..
- De La Mota Peynado A, Lee S, Pierce B, Wani P, Singh C, Roelofs J. The proteasome-associated protein Ecm29 inhibits proteasomal ATPase activity and in vivo protein degradation by the proteasome. J Biol Chem. 2013;288:29467-81 pubmed publisher..We propose that the inhibitory ability of Ecm29 is important for its function as a proteasome quality control factor by ensuring that aberrant proteasomes recognized by Ecm29 are inactive. ..
- Chen L, Madura K. Centrin/Cdc31 is a novel regulator of protein degradation. Mol Cell Biol. 2008;28:1829-40 pubmed..These findings reveal for the first time a new role for centrin/Cdc31 in protein degradation. ..
- Funakoshi M, Hochstrasser M. Small epitope-linker modules for PCR-based C-terminal tagging in Saccharomyces cerevisiae. Yeast. 2009;26:185-92 pubmed publisher..The set of plasmids has been deposited in the non-profit plasmid repository Addgene (http://www.addgene.org). ..
- Saeki Y, Isono E, Toh e A. Preparation of ubiquitinated substrates by the PY motif-insertion method for monitoring 26S proteasome activity. Methods Enzymol. 2005;399:215-27 pubmed..In this communication, we describe that Sic1 was successfully ubiquitinated by the PY motif-insertion method and demonstrate that Sic1 thus ubiquitinated was degraded by the purified yeast 26S proteasome. ..
- Russell S, Steger K, Johnston S. Subcellular localization, stoichiometry, and protein levels of 26 S proteasome subunits in yeast. J Biol Chem. 1999;274:21943-52 pubmed..The subcellular localization of two ATPase components of the regulatory complex of the proteasome, Sug2/Rpt4 and Sug1/Rpt6, and a subunit of the 20 S proteasome, Pre1, were determined by immunofluorescence...
- Russell S, Reed S, Huang W, Friedberg E, Johnston S. The 19S regulatory complex of the proteasome functions independently of proteolysis in nucleotide excision repair. Mol Cell. 1999;3:687-95 pubmed..Surprisingly, blockage of protein degradation by the proteasome has no effect on the efficiency of NER. This establishes that the regulatory complex of the proteasome has a function independent of protein degradation. ..
- Desany B, Alcasabas A, Bachant J, Elledge S. Recovery from DNA replicational stress is the essential function of the S-phase checkpoint pathway. Genes Dev. 1998;12:2956-70 pubmed..We propose that this checkpoint pathway plays an important role in the maintenance of DNA synthetic capabilities when DNA replication is stressed. ..
- Luan B, Huang X, Wu J, Mei Z, Wang Y, Xue X, et al. Structure of an endogenous yeast 26S proteasome reveals two major conformational states. Proc Natl Acad Sci U S A. 2016;113:2642-7 pubmed publisher..Structure-guided biochemical analysis reveals enhanced deubiquitylating enzyme activity of Rpn11 upon assembly of the lid. Our structures serve as a molecular basis for mechanistic understanding of proteasome function. ..
- Bashore C, Dambacher C, Goodall E, Matyskiela M, Lander G, Martin A. Ubp6 deubiquitinase controls conformational dynamics and substrate degradation of the 26S proteasome. Nat Struct Mol Biol. 2015;22:712-9 pubmed publisher..Ubp6 may thus act as a ubiquitin-dependent 'timer' to coordinate individual processing steps at the proteasome and modulate substrate degradation. ..
- Ding Z, Fu Z, Xu C, Wang Y, Wang Y, Li J, et al. High-resolution cryo-EM structure of the proteasome in complex with ADP-AlFx. Cell Res. 2017;27:373-385 pubmed publisher..Our results provide new insights into the mechanisms of nucleotide-driven allosteric cooperativity of the complex and of the substrate processing by the proteasome. ..
- Hatanaka A, Chen B, Sun J, Mano Y, Funakoshi M, Kobayashi H, et al. Fub1p, a novel protein isolated by boundary screening, binds the proteasome complex. Genes Genet Syst. 2011;86:305-14 pubmed..Finally, boundary assay showed that human PSMF1 also exhibited boundary establishment activity in yeast. Our results defined the functional correlation between Fub1p and PSMF1. ..
- Kimura Y, Saeki Y, Yokosawa H, Polevoda B, Sherman F, Hirano H. N-Terminal modifications of the 19S regulatory particle subunits of the yeast proteasome. Arch Biochem Biophys. 2003;409:341-8 pubmed..By using nat1, nat3, and mak3 deletion mutants, we found that 8 subunits, Rpt4, Rpt5, Rpt6, Rpn2, Rpn3, Rpn5, Rpn6, and Rpn8, were NatA substrates, and that 2 subunits, Rpt3 and Rpn11, were NatB ..
- Satoh T, Saeki Y, Hiromoto T, Wang Y, Uekusa Y, Yagi H, et al. Structural basis for proteasome formation controlled by an assembly chaperone nas2. Structure. 2014;22:731-43 pubmed publisher..Thus, Nas2 operates as a proteasome activation blocker, offering a checkpoint during the formation of the 19S ATPase prior to its docking onto the proteolytic 20S core particle. ..
- Saeki Y, Toh e A, Kudo T, Kawamura H, Tanaka K. Multiple proteasome-interacting proteins assist the assembly of the yeast 19S regulatory particle. Cell. 2009;137:900-13 pubmed publisher..Our results indicate that the RP assembly is a highly organized and elaborate process orchestrated by multiple proteasome-dedicated chaperones. ..
- Russell S, Sathyanarayana U, Johnston S. Isolation and characterization of SUG2. A novel ATPase family component of the yeast 26 S proteasome. J Biol Chem. 1996;271:32810-7 pubmed..We have now cloned the gene defined by the second complementation group. SUG2 encodes an essential 49-kDa protein that is also a member of the CAD family and is 43% identical to SUG1...