Results 1 to 10 of about 851 (94)

Cold Orthogonal Translation: A Psychrophilic Pyrrolysyl‐tRNA Synthetase Boosts Genetic Code Expansion in E. coli [PDF]

Advanced Science
Orthogonal translation systems (OTSs) enable site‐specific incorporation of non‐canonical amino acids (ncAAs) and are central to genetic code expansion.
Nikolaj G. Koch, Peter Goettig, Michael A. Nash, Juri Rappsilber, Nediljko Budisa   +4 more
doaj   +3 more sources

Efficient Unnatural Protein Production by Pyrrolysyl-tRNA Synthetase With Genetically Fused Solubility Tags [PDF]

Frontiers in Bioengineering and Biotechnology, 2021
Introducing non-canonical amino acids (ncAAs) by engineered orthogonal pairs of aminoacyl-tRNA synthetases and tRNAs has proven to be a highly useful tool for the expansion of the genetic code.
Nikolaj G. Koch, Nikolaj G. Koch, Tobias Baumann, Nediljko Budisa, Nediljko Budisa   +4 more
doaj   +2 more sources

Directed Evolution of Methanomethylophilus alvus Pyrrolysyl-tRNA Synthetase Generates a Hyperactive and Highly Selective Variant [PDF]

Frontiers in Molecular Biosciences, 2022
Pyrrolysyl-tRNA synthetase (PylRS) is frequently used for site-specific incorporation of noncanonical amino acids (ncAAs) into proteins. Recently, the active site of Methanomethylophilus alvus PylRS (MaPylRS) has been rationally engineered to expand its ...
Jonathan T. Fischer, Dieter Söll, Dieter Söll, Jeffery M. Tharp   +3 more
doaj   +2 more sources

Enhancing the performance of a mutant pyrrolysyl-tRNA synthetase to create a highly versatile eukaryotic cell-free protein synthesis tool [PDF]

Scientific Reports, 2023
Modification of proteins with a broad range of chemical functionalities enables the investigation of protein structure and activity by manipulating polypeptides at single amino acid resolution.
Jeffrey L. Schloßhauer, Anne Zemella, Srujan K. Dondapati, Lena Thoring, Manpreet Meyer, Stefan Kubick   +5 more
doaj   +2 more sources

An evolved pyrrolysyl-tRNA synthetase with polysubstrate specificity expands the toolbox for engineering enzymes with incorporation of noncanonical amino acids [PDF]

Bioresources and Bioprocessing, 2023
Aminoacyl-tRNA synthetase (aaRS) is a core component for genetic code expansion (GCE), a powerful technique that enables the incorporation of noncanonical amino acids (ncAAs) into a protein. The aaRS with polyspecificity can be exploited in incorporating
Ke Liu, Ling Jiang, Shuang Ma, Zhongdi Song, Lun Wang, Qunfeng Zhang, Renhao Xu, Lirong Yang, Jianping Wu, Haoran Yu   +9 more
doaj   +2 more sources

Ferritin Conjugates With Multiple Clickable Amino Acids Encoded by C-Terminal Engineered Pyrrolysyl-tRNA Synthetase [PDF]

Frontiers in Chemistry, 2021
This study reports the application of expanding genetic codes in developing protein cage-based delivery systems. The evolved Methanosarcina mazei pyrrolysyl-tRNA synthetase (PylRS)•tRNAPyl pairs derived from directed evolution are examined to probe their
Yi-Hui Wang, Mu-Lung Jian, Mu-Lung Jian, Pei-Jung Chen, Pei-Jung Chen, Jo-Chu Tsou, Jo-Chu Tsou, Le P. Truong, Yane-Shih Wang, Yane-Shih Wang   +9 more
doaj   +2 more sources

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

Nature Communications, 2020
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
Wenlong Ding, Hongxia Zhao, Yulin Chen, Bin Zhang, Yang Yang, Jia Zang, Jing Wu, Shixian Lin   +7 more
doaj   +2 more sources

Machine learning-guided evolution of pyrrolysyl-tRNA synthetase for improved incorporation efficiency of diverse noncanonical amino acids [PDF]

Nature Communications
The pyrrolysyl-tRNA synthetase (PylRS) is widely used to incorporate noncanonical amino acids (ncAAs) into proteins. However, the yields of most ncAA-containing protein  remain low due to the limited activity of PylRS variants.
Qunfeng Zhang, Ling Jiang, Yadan Niu, Yujie Li, Wanyi Chen, Jingxi Cheng, Haote Ding, Binbin Chen, Ke Liu, Jiawen Cao, Junli Wang, Shilin Ye, Lirong Yang, Jianping Wu, Gang Xu, Jianping Lin, Haoran Yu   +16 more
doaj   +2 more sources

Unraveling Synthetase's Mode of Action: The Pyrrolysyl-tRNA Synthetase Dimer Uses Secondary Binding Sites in the Cell. [PDF]

Angew Chem Int Ed Engl
The pyrrolysyl‐tRNA synthetase dimer exhibits an alternating mode of action of its monomers within its catalytic cycle, which is realized upon occupation of secondary binding sites located at the intermonomer interfaces outside the catalytic binding site.
Dröden J, Globisch C, Landwehr E, Braun TS, Summerer D, Peter C, Drescher M.   +6 more
europepmc   +2 more sources

Pyrrolysyl-tRNA Synthetase with a Unique Architecture Enhances the Availability of Lysine Derivatives in Synthetic Genetic Codes [PDF]

Molecules, 2018
Genetic code expansion has largely relied on two types of the tRNA—aminoacyl-tRNA synthetase pairs. One involves pyrrolysyl-tRNA synthetase (PylRS), which is used to incorporate various lysine derivatives into proteins.
Atsushi Yamaguchi, Fumie Iraha, Kazumasa Ohtake, Kensaku Sakamoto   +3 more
doaj   +2 more sources