Domain structure in yeast tRNA ligase
- Creators
- Xu, Qi
- Teplow, David
- Lee, Terry D.
- Abelson, John
Abstract
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.
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.Additional details
- Eprint ID
- 81610
- DOI
- 10.1021/bi00478a004
- Resolver ID
- CaltechAUTHORS:20170920-094930719
- NIH
- American Cancer Society
- Created
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2017-09-20Created from EPrint's datestamp field
- Updated
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2021-11-15Created from EPrint's last_modified field