Expanding the genetic code with a lysine derivative bearing an enzymatically removable phenylacetyl group

Marie Reille-Seroussi; Susanne V. Mayer; Wolfgang Dörner; Kathrin Lang; Henning D. Mootz

doi:10.1039/c9cc00475k

Expanding the genetic code with a lysine derivative bearing an enzymatically removable phenylacetyl group

Marie Reille-Seroussi, Susanne V. Mayer, Wolfgang Dörner, Kathrin Lang, Henning D. Mootz

Department of Bioscience

Research output: Contribution to journal › Article › peer-review

7 Scopus citations

Abstract

We report the genetically encoded incorporation of phenylacetyl protected lysine (PacK) into proteins in Escherichia coli. This unnatural side-chain modification can be enzymatically removed using either penicillin G acylase (PGA) or, surprisingly, the sirtuin SrtN from Bacillus subtilis. Our approach expands the toolbox to reversibly control protein structure and function under very mild and non-denaturing conditions, as demonstrated by triggering the activity of the nonribosomal peptide synthetase GrsA.

Original language	English
Pages (from-to)	4793-4796
Number of pages	4
Journal	Chemical Communications
Volume	55
Issue number	33
DOIs	https://doi.org/10.1039/c9cc00475k
State	Published - 2019

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abstract = "We report the genetically encoded incorporation of phenylacetyl protected lysine (PacK) into proteins in Escherichia coli. This unnatural side-chain modification can be enzymatically removed using either penicillin G acylase (PGA) or, surprisingly, the sirtuin SrtN from Bacillus subtilis. Our approach expands the toolbox to reversibly control protein structure and function under very mild and non-denaturing conditions, as demonstrated by triggering the activity of the nonribosomal peptide synthetase GrsA.",

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AU - Reille-Seroussi, Marie

AU - Mayer, Susanne V.

AU - Dörner, Wolfgang

AU - Lang, Kathrin

AU - Mootz, Henning D.

N1 - Publisher Copyright: © The Royal Society of Chemistry.

PY - 2019

Y1 - 2019

N2 - We report the genetically encoded incorporation of phenylacetyl protected lysine (PacK) into proteins in Escherichia coli. This unnatural side-chain modification can be enzymatically removed using either penicillin G acylase (PGA) or, surprisingly, the sirtuin SrtN from Bacillus subtilis. Our approach expands the toolbox to reversibly control protein structure and function under very mild and non-denaturing conditions, as demonstrated by triggering the activity of the nonribosomal peptide synthetase GrsA.

AB - We report the genetically encoded incorporation of phenylacetyl protected lysine (PacK) into proteins in Escherichia coli. This unnatural side-chain modification can be enzymatically removed using either penicillin G acylase (PGA) or, surprisingly, the sirtuin SrtN from Bacillus subtilis. Our approach expands the toolbox to reversibly control protein structure and function under very mild and non-denaturing conditions, as demonstrated by triggering the activity of the nonribosomal peptide synthetase GrsA.

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U2 - 10.1039/c9cc00475k

DO - 10.1039/c9cc00475k

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VL - 55

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JO - Chemical Communications

JF - Chemical Communications

IS - 33

ER -

Expanding the genetic code with a lysine derivative bearing an enzymatically removable phenylacetyl group

Abstract

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