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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Domain structure in yeast tRNA ligase.

Yeast tRNA ligase is one of two proteins required for the splicing of precursor tRNA molecules containing introns. The 95-kDa tRNA ligase has been purified to homogeneity from a strain of Escherichia coli which overexpresses the protein. The ligation reaction requires three enzymatic activities: phosphodiesterase, polynucleotide kinase, and ligase. By partial proteolytic digestion, we have produced fragments of tRNA ligase which contain the constituent activities. These results provide evidence for a model in which the three constituent activities of ligase are located in three distinct domains separated by protease-sensitive regions. We have also located the active adenylylated site in the ligase domains. It is lysine-114. The tRNA ligase sequence in this region has limited homology to the active-site region of T4 RNA ligase.[1]


  1. Domain structure in yeast tRNA ligase. Xu, Q., Teplow, D., Lee, T.D., Abelson, J. Biochemistry (1990) [Pubmed]
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