Synthesis and screening of a CaaL peptide library versus FTase reveals a surprising number of substrates

Amanda J. Krzysiak; Animesh V. Aditya; James L. Hougland; Carol A. Fierke; Richard A. Gibbs

doi:10.1016/j.bmcl.2009.11.011

Synthesis and screening of a CaaL peptide library versus FTase reveals a surprising number of substrates

Amanda J. Krzysiak, Animesh V. Aditya, James L. Hougland, Carol A. Fierke, Richard A. Gibbs

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

23 Scopus citations

Abstract

Proteins bearing a CaaL sequence are typically geranylgeranylated to enable their proper localization and function. We found that many of the dansyl-GCaaL peptides representing mammalian CaaL proteins can be farnesylated by FTase. This result may have important implications for prenylated protein biology.

Original language	English (US)
Pages (from-to)	767-770
Number of pages	4
Journal	Bioorganic and Medicinal Chemistry Letters
Volume	20
Issue number	2
DOIs	https://doi.org/10.1016/j.bmcl.2009.11.011
State	Published - Jan 15 2010
Externally published	Yes

Keywords

Enzymes
Farnesylation
Geranylgeranylation
Peptide synthesis
Post-translational modification

ASJC Scopus subject areas

Biochemistry
Molecular Medicine
Molecular Biology
Pharmaceutical Science
Drug Discovery
Clinical Biochemistry
Organic Chemistry

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10.1016/j.bmcl.2009.11.011

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title = "Synthesis and screening of a CaaL peptide library versus FTase reveals a surprising number of substrates",

abstract = "Proteins bearing a CaaL sequence are typically geranylgeranylated to enable their proper localization and function. We found that many of the dansyl-GCaaL peptides representing mammalian CaaL proteins can be farnesylated by FTase. This result may have important implications for prenylated protein biology.",

keywords = "Enzymes, Farnesylation, Geranylgeranylation, Peptide synthesis, Post-translational modification",

author = "Krzysiak, {Amanda J.} and Aditya, {Animesh V.} and Hougland, {James L.} and Fierke, {Carol A.} and Gibbs, {Richard A.}",

note = "Funding Information: This work was supported by NIH grants R01CA78819 (R.A.G.), R01GM40602 (C.A.F.), F32GM78894 (J.L.H.), and P30 CA21368 (Purdue Center for Cancer Research). A.J.K. and A.V.A. were supported in part by PRF fellowships.",

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T1 - Synthesis and screening of a CaaL peptide library versus FTase reveals a surprising number of substrates

AU - Krzysiak, Amanda J.

AU - Aditya, Animesh V.

AU - Hougland, James L.

AU - Fierke, Carol A.

AU - Gibbs, Richard A.

N1 - Funding Information: This work was supported by NIH grants R01CA78819 (R.A.G.), R01GM40602 (C.A.F.), F32GM78894 (J.L.H.), and P30 CA21368 (Purdue Center for Cancer Research). A.J.K. and A.V.A. were supported in part by PRF fellowships.

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Y1 - 2010/1/15

N2 - Proteins bearing a CaaL sequence are typically geranylgeranylated to enable their proper localization and function. We found that many of the dansyl-GCaaL peptides representing mammalian CaaL proteins can be farnesylated by FTase. This result may have important implications for prenylated protein biology.

AB - Proteins bearing a CaaL sequence are typically geranylgeranylated to enable their proper localization and function. We found that many of the dansyl-GCaaL peptides representing mammalian CaaL proteins can be farnesylated by FTase. This result may have important implications for prenylated protein biology.

KW - Enzymes

KW - Farnesylation

KW - Geranylgeranylation

KW - Peptide synthesis

KW - Post-translational modification

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Synthesis and screening of a CaaL peptide library versus FTase reveals a surprising number of substrates

Abstract

Keywords

ASJC Scopus subject areas

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