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Domain structure in yeast tRNA ligase

Xu, Qi and Teplow, David and Lee, Terry D. and Abelson, John (1990) Domain structure in yeast tRNA ligase. Biochemistry, 29 (26). pp. 6132-6138. ISSN 0006-2960. doi:10.1021/bi00478a004.

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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.

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Additional Information:© 1990 American Chemical Society. Received January 23, 1990; Revised Manuscript Received March 15, 1990. This work was supported by grants (to J.A.) from the NIH and the American Cancer Society. We thank Kyle Tanner, Shawn Westaway, and Chris Greer for their advice during this project and for criticisms of the paper. Haul Wong provided expert assistance in protein sequence determination.
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American Cancer SocietyUNSPECIFIED
Issue or Number:26
Record Number:CaltechAUTHORS:20170920-094930719
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Official Citation:Domain structure in yeast tRNA ligase Qi Xu, David Teplow, Terry D. Lee, and John Abelson Biochemistry 1990 29 (26), 6132-6138 DOI: 10.1021/bi00478a004
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:81610
Deposited By: Tony Diaz
Deposited On:20 Sep 2017 19:05
Last Modified:15 Nov 2021 19:44

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