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Proteins from Thermophilic Thermus thermophilus Often Do Not Fold Correctly in a Mesophilic Expression System Such as Escherichia coli
[Image: see text] Majority of protein structure studies use Escherichia coli (E. coli) and other model organisms as expression systems for other species’ genes. However, protein folding depends on cellular environment factors, such as chaperone proteins, cytoplasmic pH, temperature, and ionic concen...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical Society
2022
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9608423/ https://www.ncbi.nlm.nih.gov/pubmed/36312379 http://dx.doi.org/10.1021/acsomega.2c04786 |
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author | Kruglikov, Alibek Wei, Yulong Xia, Xuhua |
author_facet | Kruglikov, Alibek Wei, Yulong Xia, Xuhua |
author_sort | Kruglikov, Alibek |
collection | PubMed |
description | [Image: see text] Majority of protein structure studies use Escherichia coli (E. coli) and other model organisms as expression systems for other species’ genes. However, protein folding depends on cellular environment factors, such as chaperone proteins, cytoplasmic pH, temperature, and ionic concentrations. Because of differences in these factors, especially temperature and chaperones, native proteins in organisms such as extremophiles may fold improperly when they are expressed in mesophilic model organisms. Here we present a methodology of assessing the effects of using E. coli as the expression system on protein structures. We compare these effects between eight mesophilic bacteria and Thermus thermophilus (T. thermophilus), a thermophile, and found that differences are significantly larger for T. thermophilus. More specifically, helical secondary structures in T. thermophilus proteins are often replaced by coil structures in E. coli. Our results show unique directionality in misfolding when proteins in thermophiles are expressed in mesophiles. This indicates that extremophiles, such as thermophiles, require unique protein expression systems in protein folding studies. |
format | Online Article Text |
id | pubmed-9608423 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | American Chemical Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-96084232022-10-28 Proteins from Thermophilic Thermus thermophilus Often Do Not Fold Correctly in a Mesophilic Expression System Such as Escherichia coli Kruglikov, Alibek Wei, Yulong Xia, Xuhua ACS Omega [Image: see text] Majority of protein structure studies use Escherichia coli (E. coli) and other model organisms as expression systems for other species’ genes. However, protein folding depends on cellular environment factors, such as chaperone proteins, cytoplasmic pH, temperature, and ionic concentrations. Because of differences in these factors, especially temperature and chaperones, native proteins in organisms such as extremophiles may fold improperly when they are expressed in mesophilic model organisms. Here we present a methodology of assessing the effects of using E. coli as the expression system on protein structures. We compare these effects between eight mesophilic bacteria and Thermus thermophilus (T. thermophilus), a thermophile, and found that differences are significantly larger for T. thermophilus. More specifically, helical secondary structures in T. thermophilus proteins are often replaced by coil structures in E. coli. Our results show unique directionality in misfolding when proteins in thermophiles are expressed in mesophiles. This indicates that extremophiles, such as thermophiles, require unique protein expression systems in protein folding studies. American Chemical Society 2022-10-14 /pmc/articles/PMC9608423/ /pubmed/36312379 http://dx.doi.org/10.1021/acsomega.2c04786 Text en © 2022 The Authors. Published by American Chemical Society https://creativecommons.org/licenses/by-nc-nd/4.0/Permits non-commercial access and re-use, provided that author attribution and integrity are maintained; but does not permit creation of adaptations or other derivative works (https://creativecommons.org/licenses/by-nc-nd/4.0/). |
spellingShingle | Kruglikov, Alibek Wei, Yulong Xia, Xuhua Proteins from Thermophilic Thermus thermophilus Often Do Not Fold Correctly in a Mesophilic Expression System Such as Escherichia coli |
title | Proteins from Thermophilic Thermus thermophilus Often Do Not Fold Correctly in a Mesophilic
Expression System Such
as Escherichia coli |
title_full | Proteins from Thermophilic Thermus thermophilus Often Do Not Fold Correctly in a Mesophilic
Expression System Such
as Escherichia coli |
title_fullStr | Proteins from Thermophilic Thermus thermophilus Often Do Not Fold Correctly in a Mesophilic
Expression System Such
as Escherichia coli |
title_full_unstemmed | Proteins from Thermophilic Thermus thermophilus Often Do Not Fold Correctly in a Mesophilic
Expression System Such
as Escherichia coli |
title_short | Proteins from Thermophilic Thermus thermophilus Often Do Not Fold Correctly in a Mesophilic
Expression System Such
as Escherichia coli |
title_sort | proteins from thermophilic thermus thermophilus often do not fold correctly in a mesophilic
expression system such
as escherichia coli |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9608423/ https://www.ncbi.nlm.nih.gov/pubmed/36312379 http://dx.doi.org/10.1021/acsomega.2c04786 |
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