Methyltransferase-like protein 16 binds the 3′-terminal triple helix of MALAT1 long noncoding RNA
Brown JA, Kinzig CG, DeGregorio SJ, Steitz JA. Methyltransferase-like protein 16 binds the 3′-terminal triple helix of MALAT1 long noncoding RNA. Proceedings Of The National Academy Of Sciences Of The United States Of America 2016, 113: 14013-14018. PMID: 27872311, PMCID: PMC5150381, DOI: 10.1073/pnas.1614759113.Peer-Reviewed Original ResearchConceptsGel shift assaysMetastasis-associated lung adenocarcinoma transcript 1RNA triple helicesPutative RNA methyltransferaseCompetitive gel shift assaysRNA-protein interactionsRNA stability elementAbundant nuclear proteinNative gel shift assaysRich internal loopSitu proximity ligation assayTriple helixHEK293T cell lysatesStem-loop structureProximity ligation assayT cell lysatesRNA methyltransferaseVivo UVNucleotide compositionNuclear proteinsLung adenocarcinoma transcript 1RNA immunoprecipitationStability elementMETTL16Rich tractHoogsteen-position pyrimidines promote the stability and function of the MALAT1 RNA triple helix
Brown JA, Kinzig CG, DeGregorio SJ, Steitz JA. Hoogsteen-position pyrimidines promote the stability and function of the MALAT1 RNA triple helix. RNA 2016, 22: 743-749. PMID: 26952103, PMCID: PMC4836648, DOI: 10.1261/rna.055707.115.Peer-Reviewed Original ResearchConceptsElectrophoretic mobility shift assaysRNA triple helicesBase triplesMetastasis-associated lung adenocarcinoma transcript 1RNA stability elementMobility shift assaysTriple helixHuman metastasis-associated lung adenocarcinoma transcript 1Small molecule bindingU base triplesNucleotide compositionCellular functionsTriple-helical stabilityShift assaysLung adenocarcinoma transcript 1Stability elementEMSA resultsBiological significanceMolecule bindingRNA catalysisHelixTranscript 1Triple helix stabilityC tripleReporter