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DARTS-ASR: Differentiable Architecture Search for Multilingual Speech Recognition and Adaptation ...
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From Semi-supervised to Almost-unsupervised Speech Recognition with Very-low Resource by Jointly Learning Phonetic Structures from Audio and Text Embeddings ...
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Almost-unsupervised Speech Recognition with Close-to-zero Resource Based on Phonetic Structures Learned from Very Small Unpaired Speech and Text Data ...
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Phonetic-and-Semantic Embedding of Spoken Words with Applications in Spoken Content Retrieval ...
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Towards Unsupervised Automatic Speech Recognition Trained by Unaligned Speech and Text only ...
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Improved Audio Embeddings by Adjacency-Based Clustering with Applications in Spoken Term Detection ...
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Evolution of eukaryal tRNA-guanine transglycosylase: insight gained from the heterocyclic substrate recognition by the wild-type and mutant human and Escherichia coli tRNA-guanine transglycosylases
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Abstract:
The enzyme tRNA-guanine transglycosylase (TGT) is involved in the queuosine modification of tRNAs in eukarya and eubacteria and in the archaeosine modification of tRNAs in archaea. However, the different classes of TGTs utilize different heterocyclic substrates (and tRNA in the case of archaea). Based on the X-ray structural analyses, an earlier study [Stengl et al. (2005) Mechanism and substrate specificity of tRNA-guanine transglycosylases (TGTs): tRNA-modifying enzymes from the three different kingdoms of life share a common catalytic mechanism. Chembiochem, 6, 1926–1939] has made a compelling case for the divergent evolution of the eubacterial and archaeal TGTs. The X-ray structure of the eukaryal class of TGTs is not known. We performed sequence homology and phylogenetic analyses, and carried out enzyme kinetics studies with the wild-type and mutant TGTs from Escherichia coli and human using various heterocyclic substrates that we synthesized. Observations with the Cys145Val (E. coli) and the corresponding Val161Cys (human) TGTs are consistent with the idea that the Cys145 evolved in eubacterial TGTs to recognize preQ1 but not queuine, whereas the eukaryal equivalent, Val161, evolved for increased recognition of queuine and a concomitantly decreased recognition of preQ1. Both the phylogenetic and kinetic analyses support the conclusion that all TGTs have divergently evolved to specifically recognize their cognate heterocyclic substrates.
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Keyword:
RNA
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URL: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3074131 http://www.ncbi.nlm.nih.gov/pubmed/21131277 https://doi.org/10.1093/nar/gkq1188
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Characterization of the human tRNA-guanine transglycosylase: Confirmation of the heterodimeric subunit structure
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Evolution of Eukaryal tRNA-Guanine Transglycosylase: Insight Gained from the Characterization of the Human and Escherichia coli tRNA-Guanine Transglycosylases.
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