Cargando…

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...

Descripción completa

Detalles Bibliográficos
Autores principales: Kruglikov, Alibek, Wei, Yulong, Xia, Xuhua
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2022
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
_version_ 1784818764637798400
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
work_keys_str_mv AT kruglikovalibek proteinsfromthermophilicthermusthermophilusoftendonotfoldcorrectlyinamesophilicexpressionsystemsuchasescherichiacoli
AT weiyulong proteinsfromthermophilicthermusthermophilusoftendonotfoldcorrectlyinamesophilicexpressionsystemsuchasescherichiacoli
AT xiaxuhua proteinsfromthermophilicthermusthermophilusoftendonotfoldcorrectlyinamesophilicexpressionsystemsuchasescherichiacoli