S-Farnesylcysteine methyltransferase in bovine brain

Craig Volker; Raymond A. Miller; Jeffry B. Stock

doi:10.1016/S1046-2023(05)80329-9

S-Farnesylcysteine methyltransferase in bovine brain

Craig Volker, Raymond A. Miller, Jeffry B. Stock

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

28 Scopus citations

Abstract

Members of the ras family of GTP binding proteins, nuclear lamin B, the γ subunit of transducin, and specific yeast mating pheromones are subject to a set of post-translational modifications that culminate in methylation of the α-carboxyl group of a carboxyl-terminal S-farnesylcysteine residue. N-Acetyl-S-trans,trans-farnesyl-l-cysteine (AFC), a small molecule analog of this carboxyl-terminal amino acid, is a substrate of the carboxyl methyltransferase (K_M= ∼20 μm). Here we report the synthesis and characterization of AFC and demonstrate how we have exploited its distinctive properties to develop a rapid assay for carboxyl methyltransferase activity.

Original language	English (US)
Pages (from-to)	283-287
Number of pages	5
Journal	Methods
Volume	1
Issue number	3
DOIs	https://doi.org/10.1016/S1046-2023(05)80329-9
State	Published - Dec 1990

All Science Journal Classification (ASJC) codes

Molecular Biology
General Biochemistry, Genetics and Molecular Biology

Access to Document

10.1016/S1046-2023(05)80329-9

Cite this

@article{57e864df6c484f319add77f600258f19,

title = "S-Farnesylcysteine methyltransferase in bovine brain",

abstract = "Members of the ras family of GTP binding proteins, nuclear lamin B, the γ subunit of transducin, and specific yeast mating pheromones are subject to a set of post-translational modifications that culminate in methylation of the α-carboxyl group of a carboxyl-terminal S-farnesylcysteine residue. N-Acetyl-S-trans,trans-farnesyl-l-cysteine (AFC), a small molecule analog of this carboxyl-terminal amino acid, is a substrate of the carboxyl methyltransferase (KM= ∼20 μm). Here we report the synthesis and characterization of AFC and demonstrate how we have exploited its distinctive properties to develop a rapid assay for carboxyl methyltransferase activity.",

author = "Craig Volker and Miller, {Raymond A.} and Stock, {Jeffry B.}",

note = "Funding Information: This work was supported by grants from the United States Public Health Service (GM-08309 to C.V. and AI-20980 to J.S.) and the American Cancer Society (MV-486 to J.S.). We thank Dorothy Little for the mass spectral analysis.",

year = "1990",

month = dec,

doi = "10.1016/S1046-2023(05)80329-9",

language = "English (US)",

volume = "1",

pages = "283--287",

journal = "Methods",

issn = "1046-2023",

publisher = "Academic Press Inc.",

number = "3",

}

TY - JOUR

T1 - S-Farnesylcysteine methyltransferase in bovine brain

AU - Volker, Craig

AU - Miller, Raymond A.

AU - Stock, Jeffry B.

N1 - Funding Information: This work was supported by grants from the United States Public Health Service (GM-08309 to C.V. and AI-20980 to J.S.) and the American Cancer Society (MV-486 to J.S.). We thank Dorothy Little for the mass spectral analysis.

PY - 1990/12

Y1 - 1990/12

N2 - Members of the ras family of GTP binding proteins, nuclear lamin B, the γ subunit of transducin, and specific yeast mating pheromones are subject to a set of post-translational modifications that culminate in methylation of the α-carboxyl group of a carboxyl-terminal S-farnesylcysteine residue. N-Acetyl-S-trans,trans-farnesyl-l-cysteine (AFC), a small molecule analog of this carboxyl-terminal amino acid, is a substrate of the carboxyl methyltransferase (KM= ∼20 μm). Here we report the synthesis and characterization of AFC and demonstrate how we have exploited its distinctive properties to develop a rapid assay for carboxyl methyltransferase activity.

AB - Members of the ras family of GTP binding proteins, nuclear lamin B, the γ subunit of transducin, and specific yeast mating pheromones are subject to a set of post-translational modifications that culminate in methylation of the α-carboxyl group of a carboxyl-terminal S-farnesylcysteine residue. N-Acetyl-S-trans,trans-farnesyl-l-cysteine (AFC), a small molecule analog of this carboxyl-terminal amino acid, is a substrate of the carboxyl methyltransferase (KM= ∼20 μm). Here we report the synthesis and characterization of AFC and demonstrate how we have exploited its distinctive properties to develop a rapid assay for carboxyl methyltransferase activity.

UR - http://www.scopus.com/inward/record.url?scp=0007316628&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0007316628&partnerID=8YFLogxK

U2 - 10.1016/S1046-2023(05)80329-9

DO - 10.1016/S1046-2023(05)80329-9

M3 - Article

AN - SCOPUS:0007316628

SN - 1046-2023

VL - 1

SP - 283

EP - 287

JO - Methods

JF - Methods

IS - 3

ER -

S-Farnesylcysteine methyltransferase in bovine brain

Abstract

All Science Journal Classification (ASJC) codes

Access to Document

Other files and links

Fingerprint

Cite this