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The subcellular organisation of Saccharomyces cerevisiae

Subcellular protein localisation is essential for the mechanisms that govern cellular homeostasis. The ability to understand processes leading to this phenomenon will therefore enhance our understanding of cellular function. Here we review recent developments in this field with regard to mass spectr...

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Detalles Bibliográficos
Autores principales: Nightingale, Daniel JH, Geladaki, Aikaterini, Breckels, Lisa M, Oliver, Stephen G, Lilley, Kathryn S
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6391909/
https://www.ncbi.nlm.nih.gov/pubmed/30503867
http://dx.doi.org/10.1016/j.cbpa.2018.10.026
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author Nightingale, Daniel JH
Geladaki, Aikaterini
Breckels, Lisa M
Oliver, Stephen G
Lilley, Kathryn S
author_facet Nightingale, Daniel JH
Geladaki, Aikaterini
Breckels, Lisa M
Oliver, Stephen G
Lilley, Kathryn S
author_sort Nightingale, Daniel JH
collection PubMed
description Subcellular protein localisation is essential for the mechanisms that govern cellular homeostasis. The ability to understand processes leading to this phenomenon will therefore enhance our understanding of cellular function. Here we review recent developments in this field with regard to mass spectrometry, fluorescence microscopy and computational prediction methods. We highlight relative strengths and limitations of current methodologies focussing particularly on studies in the yeast Saccharomyces cerevisiae. We further present the first cell-wide spatial proteome map of S. cerevisiae, generated using hyperLOPIT, a mass spectrometry-based protein correlation profiling technique. We compare protein subcellular localisation assignments from this map, with two published fluorescence microscopy studies and show that confidence in localisation assignment is attained using multiple orthogonal methods that provide complementary data.
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spelling pubmed-63919092019-03-07 The subcellular organisation of Saccharomyces cerevisiae Nightingale, Daniel JH Geladaki, Aikaterini Breckels, Lisa M Oliver, Stephen G Lilley, Kathryn S Curr Opin Chem Biol Article Subcellular protein localisation is essential for the mechanisms that govern cellular homeostasis. The ability to understand processes leading to this phenomenon will therefore enhance our understanding of cellular function. Here we review recent developments in this field with regard to mass spectrometry, fluorescence microscopy and computational prediction methods. We highlight relative strengths and limitations of current methodologies focussing particularly on studies in the yeast Saccharomyces cerevisiae. We further present the first cell-wide spatial proteome map of S. cerevisiae, generated using hyperLOPIT, a mass spectrometry-based protein correlation profiling technique. We compare protein subcellular localisation assignments from this map, with two published fluorescence microscopy studies and show that confidence in localisation assignment is attained using multiple orthogonal methods that provide complementary data. Elsevier 2019-02 /pmc/articles/PMC6391909/ /pubmed/30503867 http://dx.doi.org/10.1016/j.cbpa.2018.10.026 Text en © 2018 The Authors http://creativecommons.org/licenses/by/4.0/ This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Nightingale, Daniel JH
Geladaki, Aikaterini
Breckels, Lisa M
Oliver, Stephen G
Lilley, Kathryn S
The subcellular organisation of Saccharomyces cerevisiae
title The subcellular organisation of Saccharomyces cerevisiae
title_full The subcellular organisation of Saccharomyces cerevisiae
title_fullStr The subcellular organisation of Saccharomyces cerevisiae
title_full_unstemmed The subcellular organisation of Saccharomyces cerevisiae
title_short The subcellular organisation of Saccharomyces cerevisiae
title_sort subcellular organisation of saccharomyces cerevisiae
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6391909/
https://www.ncbi.nlm.nih.gov/pubmed/30503867
http://dx.doi.org/10.1016/j.cbpa.2018.10.026
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