In vivo protein labeling with trimethoprim conjugates: A flexible chemical tag

Lawrence W. Miller, Yunfei Cai, Michael Sheetz, Virginia W. Cornish

Research output: Contribution to journalArticle

194 Citations (Scopus)

Abstract

The introduction of green fluorescent protein and its variants (GFPs) has allowed protein analysis at the level of the cell. Now, chemical methods are needed to label proteins in vivo with a wider variety of functionalities so that mechanistic questions about protein function in the complex cellular environment can be addressed. Here we demonstrate that trimethoprim derivatives can be used to selectively tag Escherichia coli dihydrofolate reductase (eDHFR) fusion proteins in wild-type mammalian cells with minimal background and fast kinetics.

Original languageEnglish (US)
Pages (from-to)255-257
Number of pages3
JournalNature Methods
Volume2
Issue number4
DOIs
StatePublished - Apr 1 2005
Externally publishedYes

Fingerprint

Trimethoprim
Proteins
Tetrahydrofolate Dehydrogenase
Green Fluorescent Proteins
Escherichia coli

ASJC Scopus subject areas

  • Biotechnology
  • Molecular Biology
  • Cell Biology

Cite this

In vivo protein labeling with trimethoprim conjugates : A flexible chemical tag. / Miller, Lawrence W.; Cai, Yunfei; Sheetz, Michael; Cornish, Virginia W.

In: Nature Methods, Vol. 2, No. 4, 01.04.2005, p. 255-257.

Research output: Contribution to journalArticle

Miller, Lawrence W. ; Cai, Yunfei ; Sheetz, Michael ; Cornish, Virginia W. / In vivo protein labeling with trimethoprim conjugates : A flexible chemical tag. In: Nature Methods. 2005 ; Vol. 2, No. 4. pp. 255-257.
@article{a2625da1519342e4a27b8d5775fd9499,
title = "In vivo protein labeling with trimethoprim conjugates: A flexible chemical tag",
abstract = "The introduction of green fluorescent protein and its variants (GFPs) has allowed protein analysis at the level of the cell. Now, chemical methods are needed to label proteins in vivo with a wider variety of functionalities so that mechanistic questions about protein function in the complex cellular environment can be addressed. Here we demonstrate that trimethoprim derivatives can be used to selectively tag Escherichia coli dihydrofolate reductase (eDHFR) fusion proteins in wild-type mammalian cells with minimal background and fast kinetics.",
author = "Miller, {Lawrence W.} and Yunfei Cai and Michael Sheetz and Cornish, {Virginia W.}",
year = "2005",
month = "4",
day = "1",
doi = "10.1038/nmeth749",
language = "English (US)",
volume = "2",
pages = "255--257",
journal = "PLoS Medicine",
issn = "1549-1277",
publisher = "Public Library of Science",
number = "4",

}

TY - JOUR

T1 - In vivo protein labeling with trimethoprim conjugates

T2 - A flexible chemical tag

AU - Miller, Lawrence W.

AU - Cai, Yunfei

AU - Sheetz, Michael

AU - Cornish, Virginia W.

PY - 2005/4/1

Y1 - 2005/4/1

N2 - The introduction of green fluorescent protein and its variants (GFPs) has allowed protein analysis at the level of the cell. Now, chemical methods are needed to label proteins in vivo with a wider variety of functionalities so that mechanistic questions about protein function in the complex cellular environment can be addressed. Here we demonstrate that trimethoprim derivatives can be used to selectively tag Escherichia coli dihydrofolate reductase (eDHFR) fusion proteins in wild-type mammalian cells with minimal background and fast kinetics.

AB - The introduction of green fluorescent protein and its variants (GFPs) has allowed protein analysis at the level of the cell. Now, chemical methods are needed to label proteins in vivo with a wider variety of functionalities so that mechanistic questions about protein function in the complex cellular environment can be addressed. Here we demonstrate that trimethoprim derivatives can be used to selectively tag Escherichia coli dihydrofolate reductase (eDHFR) fusion proteins in wild-type mammalian cells with minimal background and fast kinetics.

UR - http://www.scopus.com/inward/record.url?scp=18744406025&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=18744406025&partnerID=8YFLogxK

U2 - 10.1038/nmeth749

DO - 10.1038/nmeth749

M3 - Article

C2 - 15782216

AN - SCOPUS:18744406025

VL - 2

SP - 255

EP - 257

JO - PLoS Medicine

JF - PLoS Medicine

SN - 1549-1277

IS - 4

ER -