Pyrrolysine analogs as substrates for bacterial pyrrolysyl-tRNA synthetase in vitro and in vivo
H Katayama, K Nozawa, O Nureki… - Bioscience …, 2012 - jstage.jst.go.jp
H Katayama, K Nozawa, O Nureki, Y Nakahara, H Hojo
Bioscience, biotechnology, and biochemistry, 2012•jstage.jst.go.jpPyrrolysine-tRNAPyl complex is produced by pyrrolysyl-tRNA synthetase (PylRS). In this
study, we investigated the substrate specificity of Desulfitobacterium hafnience PylRS.
PylRS incorporated various L-lysine derivatives into tRNAPyl in vitro. In addition, the
PylRS/tRNAPyl pair introduced these lysine derivatives into the recombinant protein by the
Escherichia coli expression system, indicating that this PylRS/tRNAPyl pair can be used in
protein engineering technology.
study, we investigated the substrate specificity of Desulfitobacterium hafnience PylRS.
PylRS incorporated various L-lysine derivatives into tRNAPyl in vitro. In addition, the
PylRS/tRNAPyl pair introduced these lysine derivatives into the recombinant protein by the
Escherichia coli expression system, indicating that this PylRS/tRNAPyl pair can be used in
protein engineering technology.
Pyrrolysine-tRNAPyl complex is produced by pyrrolysyl-tRNA synthetase (PylRS). In this study, we investigated the substrate specificity of Desulfitobacterium hafnience PylRS. PylRS incorporated various L-lysine derivatives into tRNAPyl in vitro. In addition, the PylRS/tRNAPyl pair introduced these lysine derivatives into the recombinant protein by the Escherichia coli expression system, indicating that this PylRS/tRNAPyl pair can be used in protein engineering technology.
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