A Phosphorylation Tag for Uranyl Mediated Protein Purification and Photo Assisted Tag Removal

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

A Phosphorylation Tag for Uranyl Mediated Protein Purification and Photo Assisted Tag Removal. / Zhang, Qiang; Jørgensen, Thomas. J. D.; Nielsen, Peter E; Møllegaard, Niels Erik.

In: PloS one, Vol. 9, No. 3, e91138, 2014, p. 1-6.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Zhang, Q, Jørgensen, TJD, Nielsen, PE & Møllegaard, NE 2014, 'A Phosphorylation Tag for Uranyl Mediated Protein Purification and Photo Assisted Tag Removal', PloS one, vol. 9, no. 3, e91138, pp. 1-6. https://doi.org/10.1371/journal.pone.0091138

APA

Zhang, Q., Jørgensen, T. J. D., Nielsen, P. E., & Møllegaard, N. E. (2014). A Phosphorylation Tag for Uranyl Mediated Protein Purification and Photo Assisted Tag Removal. PloS one, 9(3), 1-6. [e91138]. https://doi.org/10.1371/journal.pone.0091138

Vancouver

Zhang Q, Jørgensen TJD, Nielsen PE, Møllegaard NE. A Phosphorylation Tag for Uranyl Mediated Protein Purification and Photo Assisted Tag Removal. PloS one. 2014;9(3):1-6. e91138. https://doi.org/10.1371/journal.pone.0091138

Author

Zhang, Qiang ; Jørgensen, Thomas. J. D. ; Nielsen, Peter E ; Møllegaard, Niels Erik. / A Phosphorylation Tag for Uranyl Mediated Protein Purification and Photo Assisted Tag Removal. In: PloS one. 2014 ; Vol. 9, No. 3. pp. 1-6.

Bibtex

@article{ae4b1de39bb0431da0d9844c65f35e65,
title = "A Phosphorylation Tag for Uranyl Mediated Protein Purification and Photo Assisted Tag Removal",
abstract = "Most protein purification procedures include an affinity tag fused to either the N or C-terminal end of the protein of interest as well as a procedure for tag removal. Tag removal is not straightforward and especially tag removal from the C-terminal end is a challenge due to the characteristics of enzymes available for this purpose. In the present study, we demonstrate the utility of the divalent uranyl ion in a new procedure for protein purification and tag removal. By employment of a GFP (green florescence protein) recombinant protein we show that uranyl binding to a phosphorylated C-terminal tag enables target protein purification from an E. coli extract by immobilized uranyl affinity chromatography. Subsequently, the tag can be efficiently removed by UV-irradiation assisted uranyl photocleavage. We therefore suggest that the divalent uranyl ion (UO22+) may provide a dual function in protein purification and subsequent C-terminal tag removal procedures.",
author = "Qiang Zhang and J{\o}rgensen, {Thomas. J. D.} and Nielsen, {Peter E} and M{\o}llegaard, {Niels Erik}",
year = "2014",
doi = "10.1371/journal.pone.0091138",
language = "English",
volume = "9",
pages = "1--6",
journal = "PLoS ONE",
issn = "1932-6203",
publisher = "Public Library of Science",
number = "3",

}

RIS

TY - JOUR

T1 - A Phosphorylation Tag for Uranyl Mediated Protein Purification and Photo Assisted Tag Removal

AU - Zhang, Qiang

AU - Jørgensen, Thomas. J. D.

AU - Nielsen, Peter E

AU - Møllegaard, Niels Erik

PY - 2014

Y1 - 2014

N2 - Most protein purification procedures include an affinity tag fused to either the N or C-terminal end of the protein of interest as well as a procedure for tag removal. Tag removal is not straightforward and especially tag removal from the C-terminal end is a challenge due to the characteristics of enzymes available for this purpose. In the present study, we demonstrate the utility of the divalent uranyl ion in a new procedure for protein purification and tag removal. By employment of a GFP (green florescence protein) recombinant protein we show that uranyl binding to a phosphorylated C-terminal tag enables target protein purification from an E. coli extract by immobilized uranyl affinity chromatography. Subsequently, the tag can be efficiently removed by UV-irradiation assisted uranyl photocleavage. We therefore suggest that the divalent uranyl ion (UO22+) may provide a dual function in protein purification and subsequent C-terminal tag removal procedures.

AB - Most protein purification procedures include an affinity tag fused to either the N or C-terminal end of the protein of interest as well as a procedure for tag removal. Tag removal is not straightforward and especially tag removal from the C-terminal end is a challenge due to the characteristics of enzymes available for this purpose. In the present study, we demonstrate the utility of the divalent uranyl ion in a new procedure for protein purification and tag removal. By employment of a GFP (green florescence protein) recombinant protein we show that uranyl binding to a phosphorylated C-terminal tag enables target protein purification from an E. coli extract by immobilized uranyl affinity chromatography. Subsequently, the tag can be efficiently removed by UV-irradiation assisted uranyl photocleavage. We therefore suggest that the divalent uranyl ion (UO22+) may provide a dual function in protein purification and subsequent C-terminal tag removal procedures.

U2 - 10.1371/journal.pone.0091138

DO - 10.1371/journal.pone.0091138

M3 - Journal article

C2 - 24599526

VL - 9

SP - 1

EP - 6

JO - PLoS ONE

JF - PLoS ONE

SN - 1932-6203

IS - 3

M1 - e91138

ER -

ID: 108771091