Search results for "TRNA binding"

showing 2 items of 2 documents

Mapping the tRNA binding site on the surface of human DNMT2 methyltransferase.

2012

The DNMT2 enzyme methylates tRNA-Asp at position C38. Because there is no tRNA–Dnmt2 cocrystal structure available, we have mapped the tRNA binding site of DNMT2 by systematically mutating surface-exposed lysine and arginine residues to alanine and studying the tRNA methylation activity and binding of the corresponding variants. After mutating 20 lysine and arginine residues, we identified eight of them that caused large (>4-fold) decreases in catalytic activity. These residues cluster within and next to a surface cleft in the protein, which is large enough to accommodate the tRNA anticodon loop and stem. This cleft is located next to the binding pocket for the cofactor S-adenosyl-l-methion…

Models MolecularMethyltransferaseProtein ConformationLysineMolecular Sequence DataBiologyBiochemistryMethylationCofactorRNA TransferAnimalsHumansAmino Acid SequenceDNA (Cytosine-5-)-MethyltransferasesCloning MolecularAlaninechemistry.chemical_classificationTRNA methylationBinding SitesCircular DichroismTRNA bindingEnzymeDrosophila melanogasterchemistryBiochemistryAmino Acid SubstitutionTransfer RNAbiology.proteinMutagenesis Site-DirectedNucleic Acid ConformationSequence AlignmentBiochemistry
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Kti12, a PSTK-like tRNA dependent ATPase essential for tRNA modification by Elongator

2019

Abstract Posttranscriptional RNA modifications occur in all domains of life. Modifications of anticodon bases are of particular importance for ribosomal decoding and proteome homeostasis. The Elongator complex modifies uridines in the wobble position and is highly conserved in eukaryotes. Despite recent insights into Elongator's architecture, the structure and function of its regulatory factor Kti12 have remained elusive. Here, we present the crystal structure of Kti12′s nucleotide hydrolase domain trapped in a transition state of ATP hydrolysis. The structure reveals striking similarities to an O-phosphoseryl-tRNA kinase involved in the selenocysteine pathway. Both proteins employ similar …

TRNA modificationSaccharomyces cerevisiae ProteinsProtein ConformationWobble base pairSaccharomyces cerevisiaeBiologyChaetomiumCrystallography X-Ray03 medical and health scienceschemistry.chemical_compound0302 clinical medicineRNA TransferATP hydrolysisGeneticsRNA and RNA-protein complexesAnticodonRNA Processing Post-TranscriptionalUridine030304 developmental biologyAdaptor Proteins Signal TransducingAdenosine Triphosphatases0303 health sciencesSelenocysteineRNATRNA bindingCell biologychemistryTransfer RNASelenocysteine incorporationCarrier ProteinsRibosomes030217 neurology & neurosurgery
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