Results 1 to 10 of about 810 (104)

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

qPCR assays to quantitate tRNApyl and pylRS expression in engineered cell lines.

PLoS ONE, 2019
Non-natural amino acids (nnAA) contain unique functional moieties that greatly expand the available tool set for protein engineering. But incorporation of nnAAs requires the function of an orthogonal aminoacyl tRNA synthetase/tRNA pair. Stable cell lines
Andrew Garcia, Gargi Roy, Christine Kiefer, Susan Wilson, Marcello Marelli   +4 more
doaj   +4 more sources

Attenuating RNA Viruses with Expanded Genetic Codes to Evoke Adjustable Immune Response in PylRS-${\mathbf{tRNA}}_{\mathbf{CUA}}^{\mathbf{Pyl}}$ Transgenic Mice

Vaccines, 2023
Ribonucleic acid (RNA) viruses pose heavy burdens on public-health systems. Synthetic biology holds great potential for artificially controlling their replication, a strategy that could be used to attenuate infectious viruses but is still in the ...
Zhetao Zheng, Xuesheng Wu, Yu Wang, Xu Yang, Hongmin Chen, Yuxuan Shen, Yuelin Yang, Qing Xia   +7 more
doaj   +5 more sources

Expanding the genetic code: phage-driven evolution of pyrrolysyl-synthetase for site-specific incorporation of synthetic phenylalanine and tyrosine derivatives [PDF]

Frontiers in Molecular Biosciences
IntroductionPyrrolysyl-tRNA synthetase (PylRS) is a key enzyme for the site-specific incorporation of non-canonical amino acids (ncAAs) into proteins. However, its native form has a limited substrate scope.
Anastasia Dakhnevich, Sabina Miasoutova, Danila Iliushin, Aleksey Rozanov, Roman Ivanov   +4 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

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

Genetic Encoding of a Trifunctional Photo-Cross-Linker with a Cleavable Alkyl Ester Moiety. [PDF]

Chembiochem
A novel noncanonical amino acid, DiZAAsu, possessing photo‐cross‐linking, biotinylation, and alkaline‐cleavable functionalities, is genetically encoded by an engineered pyrrolyl‐tRNA synthetase mutant. The alkyl ester moiety expands the design space of cleavable photo‐cross‐linkable amino acids.
Takayama M, Tsubota T, Yamaguchi T, Chiba K, Yoshida T, Hari Y, Tian YS, Takaya D, Mori A, Tsukamoto T, Ishimoto K, Ago Y, Okada Y, Sakamoto K, Doi T, Fukuzawa K, Obika S, Nakagawa S, Hino N.   +18 more
europepmc   +2 more sources

Expanding the Scope of Orthogonal Translation with Pyrrolysyl-tRNA Synthetases Dedicated to Aromatic Amino Acids

Molecules, 2020
In protein engineering and synthetic biology, Methanosarcina mazei pyrrolysyl-tRNA synthetase (MmPylRS), with its cognate tRNAPyl, is one of the most popular tools for site-specific incorporation of non-canonical amino acids (ncAAs).
Hsueh-Wei Tseng, Tobias Baumann, Huan Sun, Yane-Shih Wang, Zoya Ignatova, Nediljko Budisa   +5 more
doaj   +3 more sources

Development of a high yielding expression platform for the introduction of non-natural amino acids in protein sequences

mAbs, 2020
The ability to genetically encode non-natural amino acids (nnAAs) into proteins offers an expanded tool set for protein engineering. nnAAs containing unique functional moieties have enabled the study of post-translational modifications, protein ...
Gargi Roy, Jason Reier, Andrew Garcia, Tom Martin, Megan Rice, Jihong Wang, Meagan Prophet, Ronald Christie, William Dall’Acqua, Sanjeev Ahuja, Michael A Bowen, Marcello Marelli   +11 more
doaj   +3 more sources

Engineering mutually orthogonal PylRS/tRNA pairs for dual encoding of functional histidine analogues

Protein Science, 2023
AbstractThe availability of an expanded genetic code opens exciting new opportunities in enzyme design and engineering. In this regard histidine analogues have proven particularly versatile, serving as ligands to augment metalloenzyme function and as catalytic nucleophiles in designed enzymes.
Taylor, Christopher J., Hardy, Florence J., Burke, Ashleigh J., Bednar, Riley M., Mehl, Ryan A., Green, Anthony P., Lovelock, Sarah L.   +6 more
openaire   +2 more sources