M-Track: detecting short-lived protein-protein interactions in vivo

We developed a protein-proximity assay in yeast based on fusing a histone lysine methyltransferase onto a bait and its substrate onto a prey. Upon binding, the prey is stably methylated and detected by methylation-specific antibodies. We applied this approach to detect varying interaction affinities...

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Detalles Bibliográficos
Autores principales: Zuzuarregui, Aurora, Kupka, Thomas, Bhatt, Bhumika, Dohnal, Ilse, Mudrak, Ingrid, Friedmann, Christina, Schüchner, Stefan, Frohner, Ingrid E., Ammerer, Gustav, Ogris, Egon
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2012
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3428623/
https://www.ncbi.nlm.nih.gov/pubmed/22581371
http://dx.doi.org/10.1038/nmeth.2017
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author Zuzuarregui, Aurora
Kupka, Thomas
Bhatt, Bhumika
Dohnal, Ilse
Mudrak, Ingrid
Friedmann, Christina
Schüchner, Stefan
Frohner, Ingrid E.
Ammerer, Gustav
Ogris, Egon
author_facet Zuzuarregui, Aurora
Kupka, Thomas
Bhatt, Bhumika
Dohnal, Ilse
Mudrak, Ingrid
Friedmann, Christina
Schüchner, Stefan
Frohner, Ingrid E.
Ammerer, Gustav
Ogris, Egon
author_sort Zuzuarregui, Aurora
collection PubMed
description We developed a protein-proximity assay in yeast based on fusing a histone lysine methyltransferase onto a bait and its substrate onto a prey. Upon binding, the prey is stably methylated and detected by methylation-specific antibodies. We applied this approach to detect varying interaction affinities among proteins in a mitogen-activated protein kinase pathway and to detect short-lived interactions between protein phosphatase 2A and its substrates that have so far escaped direct detection.
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spelling pubmed-34286232012-12-01 M-Track: detecting short-lived protein-protein interactions in vivo Zuzuarregui, Aurora Kupka, Thomas Bhatt, Bhumika Dohnal, Ilse Mudrak, Ingrid Friedmann, Christina Schüchner, Stefan Frohner, Ingrid E. Ammerer, Gustav Ogris, Egon Nat Methods Article We developed a protein-proximity assay in yeast based on fusing a histone lysine methyltransferase onto a bait and its substrate onto a prey. Upon binding, the prey is stably methylated and detected by methylation-specific antibodies. We applied this approach to detect varying interaction affinities among proteins in a mitogen-activated protein kinase pathway and to detect short-lived interactions between protein phosphatase 2A and its substrates that have so far escaped direct detection. 2012-05-13 2012-06 /pmc/articles/PMC3428623/ /pubmed/22581371 http://dx.doi.org/10.1038/nmeth.2017 Text en Users may view, print, copy, download and text and data- mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use: http://www.nature.com/authors/editorial_policies/license.html#terms
spellingShingle Article
Zuzuarregui, Aurora
Kupka, Thomas
Bhatt, Bhumika
Dohnal, Ilse
Mudrak, Ingrid
Friedmann, Christina
Schüchner, Stefan
Frohner, Ingrid E.
Ammerer, Gustav
Ogris, Egon
M-Track: detecting short-lived protein-protein interactions in vivo
title M-Track: detecting short-lived protein-protein interactions in vivo
title_full M-Track: detecting short-lived protein-protein interactions in vivo
title_fullStr M-Track: detecting short-lived protein-protein interactions in vivo
title_full_unstemmed M-Track: detecting short-lived protein-protein interactions in vivo
title_short M-Track: detecting short-lived protein-protein interactions in vivo
title_sort m-track: detecting short-lived protein-protein interactions in vivo
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3428623/
https://www.ncbi.nlm.nih.gov/pubmed/22581371
http://dx.doi.org/10.1038/nmeth.2017
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