2018
DOI: 10.3390/molecules23102460
|View full text |Cite
|
Sign up to set email alerts
|

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

Abstract: 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. The widely used PylRS from Methanosarcinaceae comprises two distinct domains while the bacterial molecules consist of two separate polypeptides. The recently identified PylRS from Candidatus Methanomethylophilus alvus (CMaPylRS) is a single-domain, one-polypeptide enzyme that belongs to a third… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
4
1

Citation Types

1
46
0

Year Published

2018
2018
2023
2023

Publication Types

Select...
6
1

Relationship

2
5

Authors

Journals

citations
Cited by 33 publications
(47 citation statements)
references
References 35 publications
(52 reference statements)
1
46
0
Order By: Relevance
“…On the surface, the break in the base pairing of the anticodon stem as well as the lack of a connecting base between the acceptor and D-stem profile as potential identity elements for Ma tRNA Pyl . Interestingly, deletion of the unpaired nucleotide in the anticodon stem did not significantly alter the translation efficiency of Ma PylRS-tRNA Pyl in a cellfree translation system (Yamaguchi et al, 2018). Insertion of a C or U between the acceptor and D-stem (position 8) moderately decreased translation, but inserting an A or G had no effect (Yamaguchi et al, 2018).…”
Section: Allo-trnamentioning
confidence: 95%
See 3 more Smart Citations
“…On the surface, the break in the base pairing of the anticodon stem as well as the lack of a connecting base between the acceptor and D-stem profile as potential identity elements for Ma tRNA Pyl . Interestingly, deletion of the unpaired nucleotide in the anticodon stem did not significantly alter the translation efficiency of Ma PylRS-tRNA Pyl in a cellfree translation system (Yamaguchi et al, 2018). Insertion of a C or U between the acceptor and D-stem (position 8) moderately decreased translation, but inserting an A or G had no effect (Yamaguchi et al, 2018).…”
Section: Allo-trnamentioning
confidence: 95%
“…Interestingly, deletion of the unpaired nucleotide in the anticodon stem did not significantly alter the translation efficiency of Ma PylRS-tRNA Pyl in a cellfree translation system (Yamaguchi et al, 2018). Insertion of a C or U between the acceptor and D-stem (position 8) moderately decreased translation, but inserting an A or G had no effect (Yamaguchi et al, 2018). This indicates that the absence of a base in this position may not be an identity element for Ma tRNA Pyl .…”
Section: Allo-trnamentioning
confidence: 96%
See 2 more Smart Citations
“…Dh tRNA Pyl assumes a similar secondary structure to that of Mm tRNA Pyl , whereas CM a tRNA Pyl has such idiosyncrasies as no nucleotide between the acceptor and D stems, a 4-nucleotide D loop, and an extra nucleotide in the 6-base pair anticodon stem [4]. Since the removal of this extra residue does not impair the in vivo tRNA activity [18], we used the sequence of this deletion variant of CMa tRNA Pyl for the transplantation. PYLYCMa showed a higher suppression activity than PYLY1 and PYLY2, while PYLYDh was also aminoacylated by Mj TyrRS, although its suppressor activity was lower than that of PYLY1 (Table 1 and Figure S1B).…”
Section: Resultsmentioning
confidence: 99%