Yeast Complementation Assays Demonstrating the Importance of the Affinity Tag Position in Membrane Protein Purification, as Exemplified by HpUreI, the pH‐Gated Urea Channel of Helicobacter pylori

Affinity tags are a crucial component in protein purification. Despite several indications that they can influence protein structure and function, this influence is often unknown or disregarded. This unnecessarily introduces ambiguity in the interpretation of in vitro data. To illustrate that, urea...

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Main Authors: Anna Stoib, Sahar Shojaei, Christine Siligan, Andreas Horner
Format: Article
Language:English
Published: Wiley-VCH 2025-05-01
Series:Small Science
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Online Access:https://doi.org/10.1002/smsc.202400571
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author Anna Stoib
Sahar Shojaei
Christine Siligan
Andreas Horner
author_facet Anna Stoib
Sahar Shojaei
Christine Siligan
Andreas Horner
author_sort Anna Stoib
collection DOAJ
description Affinity tags are a crucial component in protein purification. Despite several indications that they can influence protein structure and function, this influence is often unknown or disregarded. This unnecessarily introduces ambiguity in the interpretation of in vitro data. To illustrate that, urea and ammonia yeast complementation assays are used as a screening tool to assess functional differences in various affinity tag positions, compared to the WT protein, using HpUreI, an acid‐gated urea channel of Helicobacter pylori. Yeast complementation assays test the pH‐dependent functionality of exogenous proteins expressed in deletion strains by observing growth. If the exogenous protein is able to replace the function of the deleted endogenous protein, yeast cells can demonstrate growth under specific assay conditions. The overall tag position and even a minor amount of residual N‐ or C‐terminal amino acids following tag cleavage exert a solute‐specific influence on HpUreI functionality, suggesting a complex solute selectivity mechanism and underscores the necessity for in vivo characterization. This cost‐effective yeast complementation assay can be adapted to test a broad range of solutes. It can be used as a preliminary screening tool for affinity tag positions or protein mutations before quantitative in vitro protein characterization.
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spelling doaj-art-52f9e383fdb948b7b6cd2f876761a4602025-08-20T03:52:29ZengWiley-VCHSmall Science2688-40462025-05-0155n/an/a10.1002/smsc.202400571Yeast Complementation Assays Demonstrating the Importance of the Affinity Tag Position in Membrane Protein Purification, as Exemplified by HpUreI, the pH‐Gated Urea Channel of Helicobacter pyloriAnna Stoib0Sahar Shojaei1Christine Siligan2Andreas Horner3Institute of Biophysics Johannes Kepler University Linz Gruberstr. 40 4020 Linz AustriaInstitute of Biophysics Johannes Kepler University Linz Gruberstr. 40 4020 Linz AustriaInstitute of Biophysics Johannes Kepler University Linz Gruberstr. 40 4020 Linz AustriaInstitute of Biophysics Johannes Kepler University Linz Gruberstr. 40 4020 Linz AustriaAffinity tags are a crucial component in protein purification. Despite several indications that they can influence protein structure and function, this influence is often unknown or disregarded. This unnecessarily introduces ambiguity in the interpretation of in vitro data. To illustrate that, urea and ammonia yeast complementation assays are used as a screening tool to assess functional differences in various affinity tag positions, compared to the WT protein, using HpUreI, an acid‐gated urea channel of Helicobacter pylori. Yeast complementation assays test the pH‐dependent functionality of exogenous proteins expressed in deletion strains by observing growth. If the exogenous protein is able to replace the function of the deleted endogenous protein, yeast cells can demonstrate growth under specific assay conditions. The overall tag position and even a minor amount of residual N‐ or C‐terminal amino acids following tag cleavage exert a solute‐specific influence on HpUreI functionality, suggesting a complex solute selectivity mechanism and underscores the necessity for in vivo characterization. This cost‐effective yeast complementation assay can be adapted to test a broad range of solutes. It can be used as a preliminary screening tool for affinity tag positions or protein mutations before quantitative in vitro protein characterization.https://doi.org/10.1002/smsc.202400571affinity tag positionsHelicobacter pyloriHp UreIpH‐gated urea channelsyeast complementation assays
spellingShingle Anna Stoib
Sahar Shojaei
Christine Siligan
Andreas Horner
Yeast Complementation Assays Demonstrating the Importance of the Affinity Tag Position in Membrane Protein Purification, as Exemplified by HpUreI, the pH‐Gated Urea Channel of Helicobacter pylori
Small Science
affinity tag positions
Helicobacter pylori
Hp UreI
pH‐gated urea channels
yeast complementation assays
title Yeast Complementation Assays Demonstrating the Importance of the Affinity Tag Position in Membrane Protein Purification, as Exemplified by HpUreI, the pH‐Gated Urea Channel of Helicobacter pylori
title_full Yeast Complementation Assays Demonstrating the Importance of the Affinity Tag Position in Membrane Protein Purification, as Exemplified by HpUreI, the pH‐Gated Urea Channel of Helicobacter pylori
title_fullStr Yeast Complementation Assays Demonstrating the Importance of the Affinity Tag Position in Membrane Protein Purification, as Exemplified by HpUreI, the pH‐Gated Urea Channel of Helicobacter pylori
title_full_unstemmed Yeast Complementation Assays Demonstrating the Importance of the Affinity Tag Position in Membrane Protein Purification, as Exemplified by HpUreI, the pH‐Gated Urea Channel of Helicobacter pylori
title_short Yeast Complementation Assays Demonstrating the Importance of the Affinity Tag Position in Membrane Protein Purification, as Exemplified by HpUreI, the pH‐Gated Urea Channel of Helicobacter pylori
title_sort yeast complementation assays demonstrating the importance of the affinity tag position in membrane protein purification as exemplified by hpurei the ph gated urea channel of helicobacter pylori
topic affinity tag positions
Helicobacter pylori
Hp UreI
pH‐gated urea channels
yeast complementation assays
url https://doi.org/10.1002/smsc.202400571
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