2025
Infection-relevant conditions dictate differential versus coordinate expression of Salmonella chaperones and cochaperones
Chan C, Mukai K, Groisman E. Infection-relevant conditions dictate differential versus coordinate expression of Salmonella chaperones and cochaperones. MBio 2025, 16: e00227-25. PMID: 40162747, PMCID: PMC12077118, DOI: 10.1128/mbio.00227-25.Peer-Reviewed Original ResearchConceptsInfection-relevant conditionsJ-domainProtein homeostasisChaperone DnaKCytoplasmic MgMolecular chaperonesNucleotide exchange factor GrpEChaperone trigger factorSigma factor RpoHProteins co-translationallyExpression of molecular chaperonesPreventing protein aggregationIncreased mRNA amountsPerturb protein homeostasisMRNA amountsCochaperone DnaJRpoH proteinCo-translationallyPost-translationallyCochaperoneExpressed genesFolded proteinsDnaKCoordinated expressionChaperoneDSP-1, the major fibronectin type-II protein of donkey seminal plasma is a small heat-shock protein and exhibits chaperone-like activity against thermal and oxidative stress
Alim S, Cheppali S, Pawar S, Swamy M. DSP-1, the major fibronectin type-II protein of donkey seminal plasma is a small heat-shock protein and exhibits chaperone-like activity against thermal and oxidative stress. Biochimica Et Biophysica Acta (BBA) - Proteins And Proteomics 2025, 1873: 141064. PMID: 39956303, DOI: 10.1016/j.bbapap.2025.141064.Peer-Reviewed Original ResearchConceptsChaperone-like activitySeminal plasmaFibronectin type IITetramer to monomersSperm capacitationSurface hydrophobicityMolecular chaperonesClient proteinsHeat shock proteinsBiophysical studiesAlcohol dehydrogenaseOxidative stressPhysiological ligandsShock proteinsProteinHead group moietySHspsBinding of phosphorylcholineCholine phospholipidsBindingFibronectinDehydrogenaseChaperoneSpermMammalsProtein Quality Control is a Master Modulator of Molecular Evolution in Bacteria
Arenas C, Alvarez M, Wilson R, Shakhnovich E, Ogbunugafor C. Protein Quality Control is a Master Modulator of Molecular Evolution in Bacteria. Genome Biology And Evolution 2025, 17: evaf010. PMID: 39837347, PMCID: PMC11789785, DOI: 10.1093/gbe/evaf010.Peer-Reviewed Original ResearchConceptsProtein quality controlMolecular evolutionProtein translation machineryProteome homeostasisTranslation machineryHost-parasite interactionsProtein spaceOrganismal developmentProtein foldingBacterial systemsCellular processesPromote proteostasisEvolutionary biologyMechanistic basesProteostasisProteinQuality controlEpistasisChaperoneProteomicsGenesBacteriaProteaseMachineryPhenotype
2024
Cab45G trafficking through the insulin secretory pathway is altered in human type 2 diabetes
Germanos M, Yau B, Taper M, Yeoman C, Wilson A, An Y, Cattin-Ortolá J, Masler D, Tong J, Naghiloo S, Needham E, van der Kraan A, Sun K, Loudovaris T, Diaz-Vegas A, Larance M, Thomas H, von Blume J, Thorn P, Ailion M, Asensio C, Kebede M. Cab45G trafficking through the insulin secretory pathway is altered in human type 2 diabetes. IScience 2024, 28: 111719. PMID: 39898024, PMCID: PMC11787600, DOI: 10.1016/j.isci.2024.111719.Peer-Reviewed Original ResearchInsulin granule biogenesisGranule biogenesisSecretory granule biogenesisSpecialized secretory cellsInsulin secretory pathwaySecretory pathwayHuman type 2 diabetesCab45Insulin granulesBiogenesisB cellsSecretory cellsHuman donor isletsPancreatic B-cellsInsulin secretionType 2 diabetesG-locallyChaperoneT2DObese humansInsulinProteinHomeostasisPathwayGranulesLimiting 20S proteasome assembly leads to unbalanced nucleo-cytoplasmic distribution of 26S/30S proteasomes and chronic proteotoxicity
Ruiz-Romero G, Berdún M, Hochstrasser M, Salas-Pino S, Daga R. Limiting 20S proteasome assembly leads to unbalanced nucleo-cytoplasmic distribution of 26S/30S proteasomes and chronic proteotoxicity. IScience 2024, 27: 111095. PMID: 39473973, PMCID: PMC11513537, DOI: 10.1016/j.isci.2024.111095.Peer-Reviewed Original ResearchProteasome assemblyDegradation of cell cycle proteinsNucleo-cytoplasmic distributionCell cycle proteinsHeat shock responseCytoplasmic proteostasisFission yeastMitotic substratesProteasome regulationCytoplasmic aggregatesUnfolded proteinsProteasome activityProteasomeConstitutive activationFunctional relevanceShock responseUmp1Cell proliferationProteinCellsCompartmentalizationAssemblyProteostasisYeastChaperoneChaperone Hsp70 helps Salmonella survive infection-relevant stress by reducing protein synthesis
Chan C, Groisman E. Chaperone Hsp70 helps Salmonella survive infection-relevant stress by reducing protein synthesis. PLOS Biology 2024, 22: e3002560. PMID: 38574172, PMCID: PMC10994381, DOI: 10.1371/journal.pbio.3002560.Peer-Reviewed Original ResearchConceptsRibosome associationProtein synthesisProtein homeostasisS. typhimuriumProtein folding capacityPreventing protein aggregationC-terminal amino acidsDomains of lifeProtein synthesis in vitroInhibit protein synthesisFolding capacityHsp70 chaperonesJ-domainSynthesis in vitroProtein foldingReduction of protein synthesisChaperone Hsp70DnaKRibosomeProtein aggregationChaperoneAmino acidsProteinStarvationHSP70
2023
Viral Evolution Shaped by Host Proteostasis Networks
Yoon J, Patrick J, Ogbunugafor C, Shoulders M. Viral Evolution Shaped by Host Proteostasis Networks. Annual Review Of Virology 2023, 10: 77-98. PMID: 37071930, PMCID: PMC10543606, DOI: 10.1146/annurev-virology-100220-112120.Peer-Reviewed Original ResearchConceptsProteostasis networkViral evolutionProtein foldingViral proteinsRegulate protein foldingViral protein productionEffective antiviral strategiesProteostasis factorsShape viral evolutionHost machineryAdaptive mutationsProtein biophysicsProtein productionFolding defectsAntiviral strategiesSequence spaceProteostasisProteinHostFoldingQuality control processChaperoneBiophysical defectsMutationsSequence
2017
Pba3‐Pba4 Plays a Role in Preventing Non‐Productive Interactions Among the α Subunits of the Proteasome
Panfair D, Ramamurthy A, Hochstrasser M, Kusmierczyk A. Pba3‐Pba4 Plays a Role in Preventing Non‐Productive Interactions Among the α Subunits of the Proteasome. The FASEB Journal 2017, 31 DOI: 10.1096/fasebj.31.1_supplement.917.1.Peer-Reviewed Original ResearchProteasome assemblyDegradation of ubiquitin-tagged proteinsMultisubunit protease complexUbiquitin-tagged proteinsNon-productive interactionsEarly eventMolecular weight complexesAssembly chaperonesTagged proteinsSubunit additionRecombinant expressionProtease complexEscherichia coliDead-end speciesProteasomeWeight complexesSubunitRing complexCoexpressionIn vivoAssemblyCrosslinking strategyChaperoneA ringSpecies
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