Crystal structures reveal an elusive functional domain of pyrrolysyl-tRNA synthetase
Abstract
Pyrrolysyl-tRNA synthetase (PylRS) is a major tool in genetic code expansion using noncanonical amino acids, yet its structure and function are not completely understood. In this work, we describe the crystal structure of the previously uncharacterized essential N-terminal domain of this unique enzyme in complex with tRNAPyl. This structure explains why PylRS remains orthogonal in a broad range of organisms, from bacteria to humans. The structure also highlights why tRNAPyl recognition by PylRS is anticodon independent: the anticodon does not contact the enzyme. Furthermore, using standard microbiological culture equipment, we established a new method for laboratory evolution—a noncontinuous counterpart of the previously developed phage-assisted continuous evolution. With this method, we evolved novel PylRS variants with enhanced activity and amino acid specificity. Finally, we employed an evolved PylRS variant to determine its N-terminal domain structure and show how its mutations improve PylRS activity in the genetic encoding of a noncanonical amino acid.
- Authors:
-
[4];
[1]
- Yale Univ., New Haven, CT (United States)
- DS Therapeutics, Houston, TX (United States); Yale Univ., New Haven, CT (United States)
- Harvard Univ., Cambridge, MA (United States)
- Academia Sinica, Taipei (Taiwan); Yale Univ., New Haven, CT (United States)
- Harvard Univ., Cambridge, MA (United States); Howard Hughes Medical Inst., Cambridge, MA (United States); Massachusetts Inst. of Technology (MIT), Cambridge, MA (United States)
- Publication Date:
- Research Org.:
- Argonne National Laboratory (ANL), Argonne, IL (United States); Yale Univ., New Haven, CT (United States)
- Sponsoring Org.:
- USDOE Office of Science (SC), Basic Energy Sciences (BES); National Institutes of Health (NIH)
- OSTI Identifier:
- 1430347
- Grant/Contract Number:
- FG02-98ER20311; AC02-06CH11357
- Resource Type:
- Accepted Manuscript
- Journal Name:
- Nature Chemical Biology
- Additional Journal Information:
- Journal Volume: 13; Journal Issue: 12; Journal ID: ISSN 1552-4450
- Publisher:
- Nature Publishing Group
- Country of Publication:
- United States
- Language:
- ENGLISH
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES
Citation Formats
Suzuki, Tateki, Miller, Corwin, Guo, Li-Tao, Ho, Joanne M. L., Bryson, David I., Wang, Yane-Shih, Liu, David R., and Söll, Dieter. Crystal structures reveal an elusive functional domain of pyrrolysyl-tRNA synthetase. United States: N. p., 2017.
Web. doi:10.1038/nchembio.2497.
Suzuki, Tateki, Miller, Corwin, Guo, Li-Tao, Ho, Joanne M. L., Bryson, David I., Wang, Yane-Shih, Liu, David R., & Söll, Dieter. Crystal structures reveal an elusive functional domain of pyrrolysyl-tRNA synthetase. United States. https://doi.org/10.1038/nchembio.2497
Suzuki, Tateki, Miller, Corwin, Guo, Li-Tao, Ho, Joanne M. L., Bryson, David I., Wang, Yane-Shih, Liu, David R., and Söll, Dieter. Mon .
"Crystal structures reveal an elusive functional domain of pyrrolysyl-tRNA synthetase". United States. https://doi.org/10.1038/nchembio.2497. https://www.osti.gov/servlets/purl/1430347.
@article{osti_1430347,
title = {Crystal structures reveal an elusive functional domain of pyrrolysyl-tRNA synthetase},
author = {Suzuki, Tateki and Miller, Corwin and Guo, Li-Tao and Ho, Joanne M. L. and Bryson, David I. and Wang, Yane-Shih and Liu, David R. and Söll, Dieter},
abstractNote = {Pyrrolysyl-tRNA synthetase (PylRS) is a major tool in genetic code expansion using noncanonical amino acids, yet its structure and function are not completely understood. In this work, we describe the crystal structure of the previously uncharacterized essential N-terminal domain of this unique enzyme in complex with tRNAPyl. This structure explains why PylRS remains orthogonal in a broad range of organisms, from bacteria to humans. The structure also highlights why tRNAPyl recognition by PylRS is anticodon independent: the anticodon does not contact the enzyme. Furthermore, using standard microbiological culture equipment, we established a new method for laboratory evolution—a noncontinuous counterpart of the previously developed phage-assisted continuous evolution. With this method, we evolved novel PylRS variants with enhanced activity and amino acid specificity. Finally, we employed an evolved PylRS variant to determine its N-terminal domain structure and show how its mutations improve PylRS activity in the genetic encoding of a noncanonical amino acid.},
doi = {10.1038/nchembio.2497},
journal = {Nature Chemical Biology},
number = 12,
volume = 13,
place = {United States},
year = {Mon Oct 16 00:00:00 EDT 2017},
month = {Mon Oct 16 00:00:00 EDT 2017}
}
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Works referencing / citing this record:
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