Featured Publications
A Conserved HEAT Domain within eIF4G Directs Assembly of the Translation Initiation Machinery
Marcotrigiano J, Lomakin I, Sonenberg N, Pestova T, Hellen C, Burley S. A Conserved HEAT Domain within eIF4G Directs Assembly of the Translation Initiation Machinery. Molecular Cell 2001, 7: 193-203. PMID: 11172724, DOI: 10.1016/s1097-2765(01)00167-8.Peer-Reviewed Original ResearchConceptsInternal ribosome entry siteTranslation initiation machineryInitiation machineryHEAT domainATP-dependent RNA helicase eIF4AStructure-based site-directed mutagenesisCap-independent translation initiationRNA helicase eIF4ASite-directed mutagenesisPicornaviral internal ribosome-entry siteRibosome entry siteRibosomal complex formationHelicase eIF4ATranslation initiationAlpha-helixEntry siteEIF4AMechanistic insightsX-ray structureComplex formationMachineryBiochemical resultsEssential componentDomainMutagenesis
2003
Transcript cleavage factors GreA and GreB act as transient catalytic components of RNA polymerase
Laptenko O, Lee J, Lomakin I, Borukhov S. Transcript cleavage factors GreA and GreB act as transient catalytic components of RNA polymerase. The EMBO Journal 2003, 22: 6322-6334. PMID: 14633991, PMCID: PMC291851, DOI: 10.1093/emboj/cdg610.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceCatalysisCross-Linking ReagentsDNA-Directed RNA PolymerasesEndoribonucleasesEscherichia coliEscherichia coli ProteinsHydroxyl RadicalModels, MolecularMolecular Sequence DataProtein ConformationProtein SubunitsSequence AlignmentSequence Homology, Amino AcidTranscription FactorsTranscription, GeneticTranscriptional Elongation FactorsConceptsN-terminal coiled-coil domainRNA polymeraseTranscription elongation factors GreANucleolytic activityRNAP secondary channelFirst transcription factorRNA hydrolysisRNAP catalytic centerCoiled-coil domainMolecular genetic methodsTerminal globular domainTranscription elongationTranscriptional pausingTranscription initiationTranscription factorsGenetic methodsKey residuesBiological roleGlobular domainCatalytic componentCatalytic centerGreAPolymeraseCatalytic actSecondary channel
2000
The Functional Role of Basic Patch, a Structural Element ofEscherichia coli Transcript Cleavage Factors GreA and GreB*
Kulish D, Lee J, Lomakin I, Nowicka B, Das A, Darst S, Normet K, Borukhov S. The Functional Role of Basic Patch, a Structural Element ofEscherichia coli Transcript Cleavage Factors GreA and GreB*. Journal Of Biological Chemistry 2000, 275: 12789-12798. PMID: 10777576, DOI: 10.1074/jbc.275.17.12789.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceDose-Response Relationship, DrugEscherichia coliEscherichia coli ProteinsGenetic Complementation TestHydrogen-Ion ConcentrationIsopropyl ThiogalactosideModels, MolecularMolecular Sequence DataMutagenesisOligonucleotidesPlasmidsRNASequence Homology, Amino AcidTemperatureTranscription FactorsTranscription, GeneticTranscriptional Elongation FactorsConceptsTernary elongation complexTranscript cleavage reactionWild-type factorBasic patchLarge basic patchFunctional roleGre proteinsThermosensitive phenotypeTranscription elongationElongation complexNascent RNAGre factorsThree-dimensional structureRNA polymeraseTerminal domainVivo functionE. coli strainsGreAGreBEscherichia coliType factorsCleavage reactionColi strainsMutantsReadthrough