Screen PDF - Nucleic Acids Research
Screen PDF - Nucleic Acids Research
Screen PDF - Nucleic Acids Research
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3612 <strong>Nucleic</strong> <strong>Acids</strong> <strong>Research</strong>, 2005, Vol. 33, No. 11Thus, we hypothesize that it is either the fixed chargingcapacity or the frozen structure of the U48C mutant thatmay be the cause of the related disease.Usually, in vitro transcription is an efficient approach tostudy the contribution of an individual nucleotide to tRNAstructure and function (6,8,24–26). Owing to the absenceof post-transcriptional modifications, different propertiesbetween the transcripts and their native counterparts werediscovered (18,27,37,38). Based on this knowledge, althoughthe hmtRNA Leu (CUN) transcript appears to fold correctlyand is aminoacyable, it mimics the native tRNA mainly atan immature level. Further in vivo study will be helpful toelucidate the mechanism of the related diseases.Figure 5. Effects of the designed mutations on aminoacylation capacity ofhmtRNA Leu (CUN). All values were the average of three experiments. Thestandard errors were