Analysis of protein prenylation in vitro and in vivo using functionalized phosphoisoprenoids

Nguyen, Uyen T.T., Wu, Yaowen, Goodall, Andrew and Alexandrov, Kirill (2010) Analysis of protein prenylation in vitro and in vivo using functionalized phosphoisoprenoids. Current Protocols in Protein Science, Unit 14 Supp.62: 14.3.1-14.3.15. doi:10.1002/0471140864.ps1403s62

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Author Nguyen, Uyen T.T.
Wu, Yaowen
Goodall, Andrew
Alexandrov, Kirill
Title Analysis of protein prenylation in vitro and in vivo using functionalized phosphoisoprenoids
Journal name Current Protocols in Protein Science   Check publisher's open access policy
ISSN 1934-3655
ISBN 9780471140863
Publication date 2010-11-01
Sub-type Article (original research)
DOI 10.1002/0471140864.ps1403s62
Volume Unit 14
Issue Supp.62
Start page 14.3.1
End page 14.3.15
Total pages 15
Place of publication Brooklyn, N.Y.
Publisher Wiley
Collection year 2011
Language eng
Abstract Post-translational modifications (PTMs) expand the number of protein isoforms in eukaryotic proteome by orders of magnitude. Protein modification with isoprenoid lipids is a common PTM affecting hundreds of proteins controlling the transport of information and materials into, through, and out of the eukaryotic cell. In this modification, a soluble phosphoisoprenoid such as farnesyl (C15) or geranylgeranyl (C20) pyrophosphate moiety is recruited by one of three protein prenyltransferases to covalently modify a C-terminal cysteine(s) in a target protein. The three mammalian prenyltransferases are farnesyltransferase (FTase), geranylgeranyltransferase type I (GGTase I), and Rab geranylgeranyl transferase (also termed geranylgeranyltransferase type II - GGTase II). In this unit, synthetic isoprenoids conjugated to either a fluorophore or biotin group are used to assay the activity of protein prenyltransferases in vitro or to affinity tag prenylatable proteins in cell lysates. These protocols and their modifications can be used to study the mechanisms of protein prenylation, identify prenylation targets, and characterize inhibitors of protein prenyltransferases in vitro and in vivo. Curr. Protoc. Protein Sci. 62:14.3.1-14.3.15. © 2010 by John Wiley & Sons, Inc.
Keyword Protein prenylation
Protein prenyltransferases
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2011 Collection
Institute for Molecular Bioscience - Publications
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Created: Wed, 23 Feb 2011, 14:38:46 EST by Susan Allen on behalf of Institute for Molecular Bioscience