2022
Insight into the Tumor Suppression Mechanism from the Structure of Human Polypyrimidine Splicing Factor (PSF/SFPQ) Complexed with a 30mer RNA from Murine Virus-like 30S Transcript‑1
Wang J, Sachpatzidis A, Christian TD, Lomakin IB, Garen A, Konigsberg WH. Insight into the Tumor Suppression Mechanism from the Structure of Human Polypyrimidine Splicing Factor (PSF/SFPQ) Complexed with a 30mer RNA from Murine Virus-like 30S Transcript‑1. Biochemistry 2022, 61: 1723-1734. PMID: 35998361, DOI: 10.1021/acs.biochem.2c00192.Peer-Reviewed Original ResearchConceptsRNA recognition motifSplicing factorsRNA bindingÅ resolution crystal structureTranscript 1DNA-binding domainRNA-binding pocketTumor suppression mechanismNew regulatory mechanismTumor suppressor proteinResolution crystal structureMurine virusesAcid proteinSuppressor proteinRecognition motifLung adenocarcinoma transcript 1Gene expressionRegulatory mechanismsApo structureRNA virusesHuman diseasesRNABinding pocketsHuman metastasesPositive cooperativity
2014
Structural insights into the stabilization of MALAT1 noncoding RNA by a bipartite triple helix
Brown JA, Bulkley D, Wang J, Valenstein ML, Yario TA, Steitz TA, Steitz JA. Structural insights into the stabilization of MALAT1 noncoding RNA by a bipartite triple helix. Nature Structural & Molecular Biology 2014, 21: 633-640. PMID: 24952594, PMCID: PMC4096706, DOI: 10.1038/nsmb.2844.Peer-Reviewed Original Research
2010
Poly(A) Tail Recognition by a Viral RNA Element Through Assembly of a Triple Helix
Mitton-Fry RM, DeGregorio SJ, Wang J, Steitz TA, Steitz JA. Poly(A) Tail Recognition by a Viral RNA Element Through Assembly of a Triple Helix. Science 2010, 330: 1244-1247. PMID: 21109672, PMCID: PMC3074936, DOI: 10.1126/science.1195858.Peer-Reviewed Original ResearchConceptsSarcoma-associated herpesvirusBox H/ACA small nucleolar RNAsMajor-groove triple helixNuclear noncoding RNANuclear retention elementSmall nucleolar RNAsViral RNA elementsRich internal loopTriple helixKaposi's sarcoma-associated herpesvirusPAN RNADeadenylation assaysRNA decayRNA clampNucleolar RNAsNoncoding RNAsNuclear RNATail recognitionRNA elementsFunctional importanceAngstrom resolutionRich loopSecondary structureRNAEne core
2005
Hydrodynamic Characterization of the DEAD-box RNA Helicase DbpA
Talavera MA, Matthews EE, Eliason WK, Sagi I, Wang J, Henn A, De La Cruz EM. Hydrodynamic Characterization of the DEAD-box RNA Helicase DbpA. Journal Of Molecular Biology 2005, 355: 697-707. PMID: 16325852, DOI: 10.1016/j.jmb.2005.10.058.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid MotifsChromatography, GelComputersCross-Linking ReagentsDEAD-box RNA HelicasesElectrophoretic Mobility Shift AssayEscherichia coliEscherichia coli ProteinsModels, BiologicalModels, MolecularProtein Structure, TertiaryRNARNA HelicasesRNA-Binding ProteinsStructural Homology, ProteinConceptsHelicase core domainNucleic acid helicasesCarboxyl-terminal domainAb initio structure prediction methodNucleic acid unwindingHelicase activityRNA metabolismHydrodynamic bead modelingDistinct RNARNA substratesHairpin 92ATP hydrolysisStructural homologyStructure prediction methodsCore domainOligomeric formsAnalytical ultracentrifugationDbpAProtein AMulti-angle laserBead modelingRNASize exclusion chromatographyKey roleFunctional properties