[HTML][HTML] Expanding the substrate scope of pyrrolysyl-transfer RNA synthetase enzymes to include non-α-amino acids in vitro and in vivo

R Fricke, CV Swenson, LT Roe, NX Hamlish, B Shah… - Nature …, 2023 - nature.com
The absence of orthogonal aminoacyl-transfer RNA (tRNA) synthetases that accept non-l-α-
amino acids is a primary bottleneck hindering the in vivo translation of sequence-defined …

Polyspecific pyrrolysyl-tRNA synthetases from directed evolution

LT Guo, YS Wang, A Nakamura… - Proceedings of the …, 2014 - National Acad Sciences
Pyrrolysyl-tRNA synthetase (PylRS) and its cognate tRNAPyl have emerged as ideal
translation components for genetic code innovation. Variants of the enzyme facilitate the …

Pyrrolysyl‐tRNA synthetase variants reveal ancestral aminoacylation function

J Ko, YS Wang, A Nakamura, LT Guo, D Söll… - FEBS …, 2013 - Wiley Online Library
Pyrrolysyl‐tRNA synthetase (PylRS) is a class IIc aminoacyl‐tRNA synthetase that is related
to phenylalanyl‐tRNA synthetase (PheRS). Genetic selection provided PylRS variants with a …

Biosynthesis of proteins incorporating a versatile set of phenylalanine analogues

K Kirshenbaum, IS Carrico, DA Tirrell - ChemBioChem, 2002 - Wiley Online Library
Macromolecular chemistry faces a dichotomy. Chemists can prepare polymers with a wide
variety of functional groups, but cannot attain the sequence-specificity and monodispersity of …

Recognition of non-α-amino substrates by pyrrolysyl-tRNA synthetase

T Kobayashi, T Yanagisawa, K Sakamoto… - Journal of molecular …, 2009 - Elsevier
Pyrrolysyl-tRNA synthetase (PylRS), an aminoacyl-tRNA synthetase (aaRS) recently found
in some methanogenic archaea and bacteria, recognizes an unusually large lysine …

Stereochemical Basis for Engineered Pyrrolysyl-tRNA Synthetase and the Efficient in Vivo Incorporation of Structurally Divergent Non-native Amino Acids

JK Takimoto, N Dellas, JP Noel, L Wang - ACS chemical biology, 2011 - ACS Publications
Unnatural amino acids (Uaas) can be translationally incorporated into proteins in vivo using
evolved tRNA/aminoacyl-tRNA synthetase (RS) pairs, affording chemistries inaccessible …

Crystal structures reveal an elusive functional domain of pyrrolysyl-tRNA synthetase

T Suzuki, C Miller, LT Guo, JML Ho, DI Bryson… - Nature chemical …, 2017 - nature.com
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 …

An Evolved Methanomethylophilus alvus Pyrrolysyl-tRNA Synthetase/tRNA Pair Is Highly Active and Orthogonal in Mammalian Cells

V Beránek, JCW Willis, JW Chin - Biochemistry, 2018 - ACS Publications
We recently characterized a new class of pyrrolysyl-tRNA synthetase (PylRS)/PyltRNA pairs
from Methanomassiliicocales that are active and orthogonal in Escherichia coli. The …

Mutually orthogonal pyrrolysyl-tRNA synthetase/tRNA pairs

JCW Willis, JW Chin - Nature chemistry, 2018 - nature.com
Genetically encoding distinct non-canonical amino acids (ncAAs) into proteins synthesized
in cells requires mutually orthogonal aminoacyl-tRNA synthetase (aaRS)/tRNA pairs. The …

[HTML][HTML] Structural basis for genetic-code expansion with bulky lysine derivatives by an engineered pyrrolysyl-tRNA synthetase

T Yanagisawa, M Kuratani, E Seki, N Hino… - Cell Chemical …, 2019 - cell.com
Pyrrolysyl-tRNA synthetase (PylRS) and tRNA Pyl have been extensively used for genetic-
code expansion. A Methanosarcina mazei PylRS mutant bearing the Y306A and Y384F …