Chemical-biological exploration of the limits of the ras de- and repalmitoylating machinery

K. Görmer; M. Bürger; J.A. Kruijtzer; I. Vetter; N. Vartak; L. Brunsveld; P.I.H. Bastiaens; R.M. Liskamp; G. Triola; H. Waldmann

doi:10.1002/cbic.201200078

Chemical-biological exploration of the limits of the ras de- and repalmitoylating machinery

K. Görmer, M. Bürger, J.A. Kruijtzer, I. Vetter, N. Vartak, L. Brunsveld, P.I.H. Bastiaens, R.M. Liskamp, G. Triola, H. Waldmann

Chemical Biology

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Abstract

A dynamic de-/repalmitoylation cycle determines localization and activity of H- and N-Ras. This combined cellular de- and repalmitoylation machinery has been shown to be substrate tolerant--it accepts variation of amino acid sequence, structure and configuration. Here, semisynthetic Ras-proteins in which the C-terminal amino acids are replaced by peptoid residues are used to reveal the first limitations of substrate recognition by the de- and repalmitoylating machinery.

Original language	English
Pages (from-to)	1017-1023
Number of pages	7
Journal	ChemBioChem
Volume	13
Issue number	7
DOIs	https://doi.org/10.1002/cbic.201200078
Publication status	Published - 2012

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AU - Kruijtzer, J.A.

AU - Vetter, I.

AU - Vartak, N.

AU - Brunsveld, L.

AU - Bastiaens, P.I.H.

AU - Liskamp, R.M.

AU - Triola, G.

AU - Waldmann, H.

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AB - A dynamic de-/repalmitoylation cycle determines localization and activity of H- and N-Ras. This combined cellular de- and repalmitoylation machinery has been shown to be substrate tolerant--it accepts variation of amino acid sequence, structure and configuration. Here, semisynthetic Ras-proteins in which the C-terminal amino acids are replaced by peptoid residues are used to reveal the first limitations of substrate recognition by the de- and repalmitoylating machinery.

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Chemical-biological exploration of the limits of the ras de- and repalmitoylating machinery

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