Cargando…
A Novel Method for Assessing the Chaperone Activity of Proteins
Protein chaperones are molecular machines which function both during homeostasis and stress conditions in all living organisms. Depending on their specific function, molecular chaperones are involved in a plethora of cellular processes by playing key roles in nascent protein chain folding, transport...
Autores principales: | , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2016
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5001627/ https://www.ncbi.nlm.nih.gov/pubmed/27564234 http://dx.doi.org/10.1371/journal.pone.0161970 |
_version_ | 1782450454287876096 |
---|---|
author | Hristozova, Nevena Tompa, Peter Kovacs, Denes |
author_facet | Hristozova, Nevena Tompa, Peter Kovacs, Denes |
author_sort | Hristozova, Nevena |
collection | PubMed |
description | Protein chaperones are molecular machines which function both during homeostasis and stress conditions in all living organisms. Depending on their specific function, molecular chaperones are involved in a plethora of cellular processes by playing key roles in nascent protein chain folding, transport and quality control. Among stress protein families–molecules expressed during adverse conditions, infection, and diseases–chaperones are highly abundant. Their molecular functions range from stabilizing stress-susceptible molecules and membranes to assisting the refolding of stress-damaged proteins, thereby acting as protective barriers against cellular damage. Here we propose a novel technique to test and measure the capability for protective activity of known and putative chaperones in a semi-high throughput manner on a plate reader. The current state of the art does not allow the in vitro measurements of chaperone activity in a highly parallel manner with high accuracy or high reproducibility, thus we believe that the method we report will be of significant benefit in this direction. The use of this method may lead to a considerable increase in the number of experimentally verified proteins with such functions, and may also allow the dissection of their molecular mechanism for a better understanding of their function. |
format | Online Article Text |
id | pubmed-5001627 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-50016272016-09-12 A Novel Method for Assessing the Chaperone Activity of Proteins Hristozova, Nevena Tompa, Peter Kovacs, Denes PLoS One Research Article Protein chaperones are molecular machines which function both during homeostasis and stress conditions in all living organisms. Depending on their specific function, molecular chaperones are involved in a plethora of cellular processes by playing key roles in nascent protein chain folding, transport and quality control. Among stress protein families–molecules expressed during adverse conditions, infection, and diseases–chaperones are highly abundant. Their molecular functions range from stabilizing stress-susceptible molecules and membranes to assisting the refolding of stress-damaged proteins, thereby acting as protective barriers against cellular damage. Here we propose a novel technique to test and measure the capability for protective activity of known and putative chaperones in a semi-high throughput manner on a plate reader. The current state of the art does not allow the in vitro measurements of chaperone activity in a highly parallel manner with high accuracy or high reproducibility, thus we believe that the method we report will be of significant benefit in this direction. The use of this method may lead to a considerable increase in the number of experimentally verified proteins with such functions, and may also allow the dissection of their molecular mechanism for a better understanding of their function. Public Library of Science 2016-08-26 /pmc/articles/PMC5001627/ /pubmed/27564234 http://dx.doi.org/10.1371/journal.pone.0161970 Text en © 2016 Hristozova et al http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. |
spellingShingle | Research Article Hristozova, Nevena Tompa, Peter Kovacs, Denes A Novel Method for Assessing the Chaperone Activity of Proteins |
title | A Novel Method for Assessing the Chaperone Activity of Proteins |
title_full | A Novel Method for Assessing the Chaperone Activity of Proteins |
title_fullStr | A Novel Method for Assessing the Chaperone Activity of Proteins |
title_full_unstemmed | A Novel Method for Assessing the Chaperone Activity of Proteins |
title_short | A Novel Method for Assessing the Chaperone Activity of Proteins |
title_sort | novel method for assessing the chaperone activity of proteins |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5001627/ https://www.ncbi.nlm.nih.gov/pubmed/27564234 http://dx.doi.org/10.1371/journal.pone.0161970 |
work_keys_str_mv | AT hristozovanevena anovelmethodforassessingthechaperoneactivityofproteins AT tompapeter anovelmethodforassessingthechaperoneactivityofproteins AT kovacsdenes anovelmethodforassessingthechaperoneactivityofproteins AT hristozovanevena novelmethodforassessingthechaperoneactivityofproteins AT tompapeter novelmethodforassessingthechaperoneactivityofproteins AT kovacsdenes novelmethodforassessingthechaperoneactivityofproteins |