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Live-cell targeting of His-tagged proteins by multivalent N-nitrilotriacetic acid carrier complexes.

Wieneke, Ralph ; Laboria, Noemi ; Rajan, Malini ; Kollmannsperger, Alina ; Natale, Francesco ; Cardoso, M. Cristina ; Tampé, Robert (2014):
Live-cell targeting of His-tagged proteins by multivalent N-nitrilotriacetic acid carrier complexes.
In: Journal of the American Chemical Society, 136 (40), pp. 13975-13978. ISSN 1520-5126,
[Article]

Abstract

The selective and fast labeling of proteins in living cells is a major challenge. Live-cell labeling techniques require a high specificity, high labeling density, and cell permeability of the tagging molecule to target the protein of interest. Here, we report on the site-specific, rapid and efficient labeling of endogenous and recombinant histidine-tagged proteins at distinct subcellular compartments using cell-penetrating multivalent chelator carrier complexes. In vivo labeling was followed in real-time in living cells, demonstrating a high specificity and high degree of colocalization in the crowded cellular environment.

Item Type: Article
Erschienen: 2014
Creators: Wieneke, Ralph ; Laboria, Noemi ; Rajan, Malini ; Kollmannsperger, Alina ; Natale, Francesco ; Cardoso, M. Cristina ; Tampé, Robert
Title: Live-cell targeting of His-tagged proteins by multivalent N-nitrilotriacetic acid carrier complexes.
Language: English
Abstract:

The selective and fast labeling of proteins in living cells is a major challenge. Live-cell labeling techniques require a high specificity, high labeling density, and cell permeability of the tagging molecule to target the protein of interest. Here, we report on the site-specific, rapid and efficient labeling of endogenous and recombinant histidine-tagged proteins at distinct subcellular compartments using cell-penetrating multivalent chelator carrier complexes. In vivo labeling was followed in real-time in living cells, demonstrating a high specificity and high degree of colocalization in the crowded cellular environment.

Journal or Publication Title: Journal of the American Chemical Society
Journal volume: 136
Number: 40
Divisions: 10 Department of Biology
10 Department of Biology > Cell Biology and Epigenetics
Date Deposited: 13 Nov 2014 08:05
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