Chimeric design of pyrrolysyl-tRNA synthetase/tRNA pairs and canonical synthetase/tRNA pairs for genetic code expansion

An orthogonal aminoacyl-tRNA synthetase/tRNA pair is a crucial prerequisite for site-specific incorporation of unnatural amino acids. Due to its high codon suppression efficiency and full orthogonality, the pyrrolysyl-tRNA synthetase/pyrrolysyl-tRNA pair is currently the ideal system for genetic cod...

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Published inNature communications Vol. 11; no. 1; pp. 3154 - 13
Main Authors Ding, Wenlong, Zhao, Hongxia, Chen, Yulin, Zhang, Bin, Yang, Yang, Zang, Jia, Wu, Jing, Lin, Shixian
Format Journal Article
LanguageEnglish
Published London Nature Publishing Group UK 22.06.2020
Nature Publishing Group
Nature Portfolio
Subjects
14/35
631/61/338/552
631/92/469
639/638/92/2783
82/58
82/80
82/83
Alanine
Alanine - analogs & derivatives
Amino acids
Amino Acids - biosynthesis
Aminoacyl-tRNA ligase
Chimera - genetics
Chimera - metabolism
Chimeras
Design
E coli
Escherichia coli
Eukaryotes
Fluorescence
Genetic Code
HEK293 Cells
Histidine
Histidine - analogs & derivatives
Humanities and Social Sciences
Humans
Lysine - analogs & derivatives
Mammalian cells
Mammals
multidisciplinary
Orthogonality
Phenylalanine
Phenylalanine - analogs & derivatives
Post-translation
Prokaryotes
RNA, Transfer - genetics
RNA, Transfer - metabolism
Science
Science (multidisciplinary)
Synthetic Biology - methods
Translation
tRNA Ala
tRNA His
Tryptophan
Tryptophan - analogs & derivatives
Tyrosine
Tyrosine - analogs & derivatives
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Abstract An orthogonal aminoacyl-tRNA synthetase/tRNA pair is a crucial prerequisite for site-specific incorporation of unnatural amino acids. Due to its high codon suppression efficiency and full orthogonality, the pyrrolysyl-tRNA synthetase/pyrrolysyl-tRNA pair is currently the ideal system for genetic code expansion in both eukaryotes and prokaryotes. There is a pressing need to discover or engineer other fully orthogonal translation systems. Here, through rational chimera design by transplanting the key orthogonal components from the pyrrolysine system, we create multiple chimeric tRNA synthetase/chimeric tRNA pairs, including chimera histidine, phenylalanine, and alanine systems. We further show that these engineered chimeric systems are orthogonal and highly efficient with comparable flexibility to the pyrrolysine system. Besides, the chimera phenylalanine system can incorporate a group of phenylalanine, tyrosine, and tryptophan analogues efficiently in both E. coli and mammalian cells. These aromatic amino acids analogous exhibit unique properties and characteristics, including fluorescence, post-translation modification. Orthogonal aminoacyl-tRNA synthetase/tRNA pairs are crucial for the incorporation of unnatural amino acids in a site-specific manner. Here the authors use rational chimera design to create multiple efficient pairs that function in bacterial and mammalian systems for genetic code expansion.
AbstractList An orthogonal aminoacyl-tRNA synthetase/tRNA pair is a crucial prerequisite for site-specific incorporation of unnatural amino acids. Due to its high codon suppression efficiency and full orthogonality, the pyrrolysyl-tRNA synthetase/pyrrolysyl-tRNA pair is currently the ideal system for genetic code expansion in both eukaryotes and prokaryotes. There is a pressing need to discover or engineer other fully orthogonal translation systems. Here, through rational chimera design by transplanting the key orthogonal components from the pyrrolysine system, we create multiple chimeric tRNA synthetase/chimeric tRNA pairs, including chimera histidine, phenylalanine, and alanine systems. We further show that these engineered chimeric systems are orthogonal and highly efficient with comparable flexibility to the pyrrolysine system. Besides, the chimera phenylalanine system can incorporate a group of phenylalanine, tyrosine, and tryptophan analogues efficiently in both E. coli and mammalian cells. These aromatic amino acids analogous exhibit unique properties and characteristics, including fluorescence, post-translation modification.
An orthogonal aminoacyl-tRNA synthetase/tRNA pair is a crucial prerequisite for site-specific incorporation of unnatural amino acids. Due to its high codon suppression efficiency and full orthogonality, the pyrrolysyl-tRNA synthetase/pyrrolysyl-tRNA pair is currently the ideal system for genetic code expansion in both eukaryotes and prokaryotes. There is a pressing need to discover or engineer other fully orthogonal translation systems. Here, through rational chimera design by transplanting the key orthogonal components from the pyrrolysine system, we create multiple chimeric tRNA synthetase/chimeric tRNA pairs, including chimera histidine, phenylalanine, and alanine systems. We further show that these engineered chimeric systems are orthogonal and highly efficient with comparable flexibility to the pyrrolysine system. Besides, the chimera phenylalanine system can incorporate a group of phenylalanine, tyrosine, and tryptophan analogues efficiently in both E. coli and mammalian cells. These aromatic amino acids analogous exhibit unique properties and characteristics, including fluorescence, post-translation modification. Orthogonal aminoacyl-tRNA synthetase/tRNA pairs are crucial for the incorporation of unnatural amino acids in a site-specific manner. Here the authors use rational chimera design to create multiple efficient pairs that function in bacterial and mammalian systems for genetic code expansion.
An orthogonal aminoacyl-tRNA synthetase/tRNA pair is a crucial prerequisite for site-specific incorporation of unnatural amino acids. Due to its high codon suppression efficiency and full orthogonality, the pyrrolysyl-tRNA synthetase/pyrrolysyl-tRNA pair is currently the ideal system for genetic code expansion in both eukaryotes and prokaryotes. There is a pressing need to discover or engineer other fully orthogonal translation systems. Here, through rational chimera design by transplanting the key orthogonal components from the pyrrolysine system, we create multiple chimeric tRNA synthetase/chimeric tRNA pairs, including chimera histidine, phenylalanine, and alanine systems. We further show that these engineered chimeric systems are orthogonal and highly efficient with comparable flexibility to the pyrrolysine system. Besides, the chimera phenylalanine system can incorporate a group of phenylalanine, tyrosine, and tryptophan analogues efficiently in both E. coli and mammalian cells. These aromatic amino acids analogous exhibit unique properties and characteristics, including fluorescence, post-translation modification.
Orthogonal aminoacyl-tRNA synthetase/tRNA pairs are crucial for the incorporation of unnatural amino acids in a site-specific manner. Here the authors use rational chimera design to create multiple efficient pairs that function in bacterial and mammalian systems for genetic code expansion.
An orthogonal aminoacyl-tRNA synthetase/tRNA pair is a crucial prerequisite for site-specific incorporation of unnatural amino acids. Due to its high codon suppression efficiency and full orthogonality, the pyrrolysyl-tRNA synthetase/pyrrolysyl-tRNA pair is currently the ideal system for genetic code expansion in both eukaryotes and prokaryotes. There is a pressing need to discover or engineer other fully orthogonal translation systems. Here, through rational chimera design by transplanting the key orthogonal components from the pyrrolysine system, we create multiple chimeric tRNA synthetase/chimeric tRNA pairs, including chimera histidine, phenylalanine, and alanine systems. We further show that these engineered chimeric systems are orthogonal and highly efficient with comparable flexibility to the pyrrolysine system. Besides, the chimera phenylalanine system can incorporate a group of phenylalanine, tyrosine, and tryptophan analogues efficiently in both E. coli and mammalian cells. These aromatic amino acids analogous exhibit unique properties and characteristics, including fluorescence, post-translation modification.An orthogonal aminoacyl-tRNA synthetase/tRNA pair is a crucial prerequisite for site-specific incorporation of unnatural amino acids. Due to its high codon suppression efficiency and full orthogonality, the pyrrolysyl-tRNA synthetase/pyrrolysyl-tRNA pair is currently the ideal system for genetic code expansion in both eukaryotes and prokaryotes. There is a pressing need to discover or engineer other fully orthogonal translation systems. Here, through rational chimera design by transplanting the key orthogonal components from the pyrrolysine system, we create multiple chimeric tRNA synthetase/chimeric tRNA pairs, including chimera histidine, phenylalanine, and alanine systems. We further show that these engineered chimeric systems are orthogonal and highly efficient with comparable flexibility to the pyrrolysine system. Besides, the chimera phenylalanine system can incorporate a group of phenylalanine, tyrosine, and tryptophan analogues efficiently in both E. coli and mammalian cells. These aromatic amino acids analogous exhibit unique properties and characteristics, including fluorescence, post-translation modification.
An orthogonal aminoacyl-tRNA synthetase/tRNA pair is a crucial prerequisite for site-specific incorporation of unnatural amino acids. Due to its high codon suppression efficiency and full orthogonality, the pyrrolysyl-tRNA synthetase/pyrrolysyl-tRNA pair is currently the ideal system for genetic code expansion in both eukaryotes and prokaryotes. There is a pressing need to discover or engineer other fully orthogonal translation systems. Here, through rational chimera design by transplanting the key orthogonal components from the pyrrolysine system, we create multiple chimeric tRNA synthetase/chimeric tRNA pairs, including chimera histidine, phenylalanine, and alanine systems. We further show that these engineered chimeric systems are orthogonal and highly efficient with comparable flexibility to the pyrrolysine system. Besides, the chimera phenylalanine system can incorporate a group of phenylalanine, tyrosine, and tryptophan analogues efficiently in both E. coli and mammalian cells. These aromatic amino acids analogous exhibit unique properties and characteristics, including fluorescence, post-translation modification.Orthogonal aminoacyl-tRNA synthetase/tRNA pairs are crucial for the incorporation of unnatural amino acids in a site-specific manner. Here the authors use rational chimera design to create multiple efficient pairs that function in bacterial and mammalian systems for genetic code expansion.
ArticleNumber 3154
Author Wu, Jing
Zang, Jia
Lin, Shixian
Ding, Wenlong
Zhang, Bin
Zhao, Hongxia
Yang, Yang
Chen, Yulin
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  organization: Life Sciences Institute, Zhejiang University
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  organization: Life Sciences Institute, Zhejiang University
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  fullname: Zhang, Bin
  organization: Life Sciences Institute, Zhejiang University
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  surname: Yang
  fullname: Yang, Yang
  organization: School of Chemistry and Chemical Engineering, Nanjing University
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  givenname: Jia
  surname: Zang
  fullname: Zang, Jia
  organization: Life Sciences Institute, Zhejiang University
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  surname: Lin
  fullname: Lin, Shixian
  email: sxlin@zju.edu.cn
  organization: Life Sciences Institute, Zhejiang University
BackLink https://www.ncbi.nlm.nih.gov/pubmed/32572025$$D View this record in MEDLINE/PubMed
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Snippet An orthogonal aminoacyl-tRNA synthetase/tRNA pair is a crucial prerequisite for site-specific incorporation of unnatural amino acids. Due to its high codon...
Orthogonal aminoacyl-tRNA synthetase/tRNA pairs are crucial for the incorporation of unnatural amino acids in a site-specific manner. Here the authors use...
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StartPage 3154
SubjectTerms 14/35
631/61/338/552
631/92/469
639/638/92/2783
82/58
82/80
82/83
Alanine
Alanine - analogs & derivatives
Amino acids
Amino Acids - biosynthesis
Aminoacyl-tRNA ligase
Chimera - genetics
Chimera - metabolism
Chimeras
Design
E coli
Escherichia coli
Eukaryotes
Fluorescence
Genetic Code
HEK293 Cells
Histidine
Histidine - analogs & derivatives
Humanities and Social Sciences
Humans
Lysine - analogs & derivatives
Mammalian cells
Mammals
multidisciplinary
Orthogonality
Phenylalanine
Phenylalanine - analogs & derivatives
Post-translation
Prokaryotes
RNA, Transfer - genetics
RNA, Transfer - metabolism
Science
Science (multidisciplinary)
Synthetic Biology - methods
Translation
tRNA Ala
tRNA His
Tryptophan
Tryptophan - analogs & derivatives
Tyrosine
Tyrosine - analogs & derivatives
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Title Chimeric design of pyrrolysyl-tRNA synthetase/tRNA pairs and canonical synthetase/tRNA pairs for genetic code expansion
URI https://link.springer.com/article/10.1038/s41467-020-16898-y
https://www.ncbi.nlm.nih.gov/pubmed/32572025
https://www.proquest.com/docview/2415569319
https://www.proquest.com/docview/2416274074
https://pubmed.ncbi.nlm.nih.gov/PMC7308279
https://doaj.org/article/6902882d572e4b6385026c9aeca8abc6
Volume 11
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