Assaying protein palmitoylation in plants

Piers A Hemsley; Laura Taylor; Claire S Grierson

doi:10.1186/1746-4811-4-2

Assaying protein palmitoylation in plants

Piers A Hemsley, Laura Taylor, Claire S Grierson

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

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Abstract

Protein S-acylation (also known as palmitoylation) is the reversible post-translational addition of acyl lipids to cysteine residues in proteins through a thioester bond. It allows strong association with membranes. Whilst prediction methods for S-acylation exist, prediction is imperfect. Existing protocols for demonstrating the S-acylation of plant proteins are either laborious and time consuming or expensive.

Original language	English
Article number	2
Journal	Plant Methods
Volume	4
Early online date	11 Jan 2008
DOIs	https://doi.org/10.1186/1746-4811-4-2
Publication status	Published - 2008

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10.1186/1746-4811-4-2

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title = "Assaying protein palmitoylation in plants",

abstract = "Protein S-acylation (also known as palmitoylation) is the reversible post-translational addition of acyl lipids to cysteine residues in proteins through a thioester bond. It allows strong association with membranes. Whilst prediction methods for S-acylation exist, prediction is imperfect. Existing protocols for demonstrating the S-acylation of plant proteins are either laborious and time consuming or expensive.",

author = "Hemsley, {Piers A} and Laura Taylor and Grierson, {Claire S}",

year = "2008",

doi = "10.1186/1746-4811-4-2",

language = "English",

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journal = "Plant Methods",

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T1 - Assaying protein palmitoylation in plants

AU - Hemsley, Piers A

AU - Taylor, Laura

AU - Grierson, Claire S

PY - 2008

Y1 - 2008

N2 - Protein S-acylation (also known as palmitoylation) is the reversible post-translational addition of acyl lipids to cysteine residues in proteins through a thioester bond. It allows strong association with membranes. Whilst prediction methods for S-acylation exist, prediction is imperfect. Existing protocols for demonstrating the S-acylation of plant proteins are either laborious and time consuming or expensive.

AB - Protein S-acylation (also known as palmitoylation) is the reversible post-translational addition of acyl lipids to cysteine residues in proteins through a thioester bond. It allows strong association with membranes. Whilst prediction methods for S-acylation exist, prediction is imperfect. Existing protocols for demonstrating the S-acylation of plant proteins are either laborious and time consuming or expensive.

U2 - 10.1186/1746-4811-4-2

DO - 10.1186/1746-4811-4-2

M3 - Article

C2 - 18190696

SN - 1746-4811

VL - 4

JO - Plant Methods

JF - Plant Methods

M1 - 2

ER -

Assaying protein palmitoylation in plants

Abstract

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