pone.0291267.s003.pdf (53.4 kB)
A PUS1D134A enzyme is catalytically inactive.
journal contribution
posted on 2023-11-08, 18:41 authored by Sebastian Grünberg, Lindsey A. Doyle, Eric J. Wolf, Nan Dai, Ivan R. Corrêa Jr., Erbay Yigit, Barry L. StoddardPercent of uridine-to-Ψ conversion as determined by LC-MS/MS of increasing concentrations of PUS1 wildtype (left) and D134A mutant (right) with the RNA oligo substrate R168 after two hours. Data of two replicas are shown.
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although recent studiesalone &# 82174 &# 197observed within trnarna bases representshelical rna duplexguide rna moleculespus &# 8217yeast pus1 boundmodify mrna transcriptscommon rna modificationrelated pus1 enzymes&# 8216pus targetinteraction withinrna targetrna containingsubsequent modificationchemical modificationpus1 recognizesxlink ">well understoodubiquitous activitythus guidestarget uridinetarget sequencesstructural requirementspseudouridine synthasemrna recognitionmodifies mrnamodel mrnahot spotenzymes includeenzyme recognizescrystal structureactive site
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