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N-Myristoyl Transferase (NMT)-Catalyzed Labeling of Bacterial Proteins for Imaging in Fixed and Live Cells

Ho, Samuel H. and Tirrell, David A. (2019) N-Myristoyl Transferase (NMT)-Catalyzed Labeling of Bacterial Proteins for Imaging in Fixed and Live Cells. In: Enzyme-Mediated Ligation Methods. Methods in Molecular Biology. No.2012. Humana Press , New York, NY, pp. 315-326. ISBN 978-1-4939-9545-5.

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Methods for selective protein imaging are critical for elucidating how cells orchestrate fundamental biological processes. We recently developed a chemoenzymatic method to modify bacterial proteins in situ for fluorescence imaging using N-myristoyl transferase (NMT). Target proteins outfitted with an N-terminal NMT recognition sequence are covalently modified with an azido fatty acid. Subsequent strain-promoted azide–alkyne cycloaddition allows for conjugation to cell-permeant fluorophores and imaging by fluorescence microscopy. Here we describe sample preparation and labeling protocols for imaging bacterial proteins in fixed and live cells.

Item Type:Book Section
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URLURL TypeDescription
Ho, Samuel H.0000-0001-7647-0752
Tirrell, David A.0000-0003-3175-4596
Additional Information:© 2019 Springer Science+Business Media, LLC, part of Springer Nature. First Online 04 June 2019.
Subject Keywords:N-Myristoyl transferase (NMT); 12-Azidododecanoic acid; Bicyclononyne–BODIPY; Escherichia coli; Site-specific; Protein labeling; Fluorescence imaging
Series Name:Methods in Molecular Biology
Issue or Number:2012
Record Number:CaltechAUTHORS:20190610-084517342
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Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:96228
Deposited By: Tony Diaz
Deposited On:10 Jun 2019 16:12
Last Modified:16 Nov 2021 17:19

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