Improved split-ubiquitin screening technique to identify surface membrane protein-protein interactions

Yeast-based methods are still the workhorse for the detection of protein-protein interactions (PPIs) in vivo. Yeast two-hybrid (Y2H) systems, however, are limited to screening for a specific group of molecules that interact in a particular cell compartment. For this reason, the split-ubiquitin syste...

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Main Authors: Daniel Ivanusic, Jürgen J. Heinisch, Magdalena Eschricht, Ulrike Laube, Joachim Denner
Format: Article
Language:English
Published: Taylor & Francis Group 2015-08-01
Series:BioTechniques
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Online Access:https://www.future-science.com/doi/10.2144/000114315
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author Daniel Ivanusic
Jürgen J. Heinisch
Magdalena Eschricht
Ulrike Laube
Joachim Denner
author_facet Daniel Ivanusic
Jürgen J. Heinisch
Magdalena Eschricht
Ulrike Laube
Joachim Denner
author_sort Daniel Ivanusic
collection DOAJ
description Yeast-based methods are still the workhorse for the detection of protein-protein interactions (PPIs) in vivo. Yeast two-hybrid (Y2H) systems, however, are limited to screening for a specific group of molecules that interact in a particular cell compartment. For this reason, the split-ubiquitin system (SUS) was developed to allow screening of cDNA libraries of full-length membrane proteins for protein-protein interactions in Saccharomyces cerevisiae. Here we demonstrate that a modification of the widely used membrane SUS involving the transmembrane (TM) domain of the yeast receptor Wsc1 increases the stringency of screening and improves the selectivity for proteins localized in the plasma membrane (PM).
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1940-9818
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publishDate 2015-08-01
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spelling doaj-art-6727c034d1ef46eea8023f028bdd51632025-08-20T02:26:06ZengTaylor & Francis GroupBioTechniques0736-62051940-98182015-08-01592637310.2144/000114315Improved split-ubiquitin screening technique to identify surface membrane protein-protein interactionsDaniel Ivanusic0Jürgen J. Heinisch1Magdalena Eschricht2Ulrike Laube3Joachim Denner41Robert Koch Institute, Berlin, Germany3Universität Osnabrück, Osnabrück, Germany1Robert Koch Institute, Berlin, Germany1Robert Koch Institute, Berlin, Germany1Robert Koch Institute, Berlin, GermanyYeast-based methods are still the workhorse for the detection of protein-protein interactions (PPIs) in vivo. Yeast two-hybrid (Y2H) systems, however, are limited to screening for a specific group of molecules that interact in a particular cell compartment. For this reason, the split-ubiquitin system (SUS) was developed to allow screening of cDNA libraries of full-length membrane proteins for protein-protein interactions in Saccharomyces cerevisiae. Here we demonstrate that a modification of the widely used membrane SUS involving the transmembrane (TM) domain of the yeast receptor Wsc1 increases the stringency of screening and improves the selectivity for proteins localized in the plasma membrane (PM).https://www.future-science.com/doi/10.2144/000114315protein-protein interactionssplit-ubiquitin systemreceptors
spellingShingle Daniel Ivanusic
Jürgen J. Heinisch
Magdalena Eschricht
Ulrike Laube
Joachim Denner
Improved split-ubiquitin screening technique to identify surface membrane protein-protein interactions
BioTechniques
protein-protein interactions
split-ubiquitin system
receptors
title Improved split-ubiquitin screening technique to identify surface membrane protein-protein interactions
title_full Improved split-ubiquitin screening technique to identify surface membrane protein-protein interactions
title_fullStr Improved split-ubiquitin screening technique to identify surface membrane protein-protein interactions
title_full_unstemmed Improved split-ubiquitin screening technique to identify surface membrane protein-protein interactions
title_short Improved split-ubiquitin screening technique to identify surface membrane protein-protein interactions
title_sort improved split ubiquitin screening technique to identify surface membrane protein protein interactions
topic protein-protein interactions
split-ubiquitin system
receptors
url https://www.future-science.com/doi/10.2144/000114315
work_keys_str_mv AT danielivanusic improvedsplitubiquitinscreeningtechniquetoidentifysurfacemembraneproteinproteininteractions
AT jurgenjheinisch improvedsplitubiquitinscreeningtechniquetoidentifysurfacemembraneproteinproteininteractions
AT magdalenaeschricht improvedsplitubiquitinscreeningtechniquetoidentifysurfacemembraneproteinproteininteractions
AT ulrikelaube improvedsplitubiquitinscreeningtechniquetoidentifysurfacemembraneproteinproteininteractions
AT joachimdenner improvedsplitubiquitinscreeningtechniquetoidentifysurfacemembraneproteinproteininteractions