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Distinct Stabilities of the Structurally Homologous Heptameric Co-Chaperonins GroES and gp31
The GroES heptamer is the molecular co-chaperonin that partners with the tetradecamer chaperonin GroEL, which assists in the folding of various nonnative polypeptide chains in Escherichia coli. Gp31 is a structural and functional analogue of GroES encoded by the bacteriophage T4, becoming highly exp...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Springer US
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6318259/ https://www.ncbi.nlm.nih.gov/pubmed/29736602 http://dx.doi.org/10.1007/s13361-018-1910-5 |
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author | Dyachenko, Andrey Tamara, Sem Heck, Albert J. R. |
author_facet | Dyachenko, Andrey Tamara, Sem Heck, Albert J. R. |
author_sort | Dyachenko, Andrey |
collection | PubMed |
description | The GroES heptamer is the molecular co-chaperonin that partners with the tetradecamer chaperonin GroEL, which assists in the folding of various nonnative polypeptide chains in Escherichia coli. Gp31 is a structural and functional analogue of GroES encoded by the bacteriophage T4, becoming highly expressed in T4-infected E. coli, taking over the role of GroES, favoring the folding of bacteriophage proteins. Despite being slightly larger, gp31 is quite homologous to GroES in terms of its tertiary and quaternary structure, as well as in its function and mode of interaction with the chaperonin GroEL. Here, we performed a side-by-side comparison of GroES and gp31 heptamer complexes by (ion mobility) tandem mass spectrometry. Surprisingly, we observed quite distinct fragmentation mechanisms for the GroES and gp31 heptamers, whereby GroES displays a unique and unusual bimodal charge distribution in its released monomers. Not only the gas-phase dissociation but also the gas-phase unfolding of GroES and gp31 were found to be very distinct. We rationalize these observations with the similar discrepancies we observed in the thermal unfolding characteristics and surface contacts within GroES and gp31 in the solution. From our data, we propose a model that explains the observed simultaneous dissociation pathways of GroES and the differences between GroES and gp31 gas-phase dissociation and unfolding. We conclude that, although GroES and gp31 exhibit high homology in tertiary and quaternary structure, they are quite distinct in their solution and gas-phase (un)folding characteristics and stability. [Figure: see text] ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1007/s13361-018-1910-5) contains supplementary material, which is available to authorized users. |
format | Online Article Text |
id | pubmed-6318259 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | Springer US |
record_format | MEDLINE/PubMed |
spelling | pubmed-63182592019-01-14 Distinct Stabilities of the Structurally Homologous Heptameric Co-Chaperonins GroES and gp31 Dyachenko, Andrey Tamara, Sem Heck, Albert J. R. J Am Soc Mass Spectrom Focus: Honoring Carol V. Robinson's Election to the National Academy of Sciences: Research Article The GroES heptamer is the molecular co-chaperonin that partners with the tetradecamer chaperonin GroEL, which assists in the folding of various nonnative polypeptide chains in Escherichia coli. Gp31 is a structural and functional analogue of GroES encoded by the bacteriophage T4, becoming highly expressed in T4-infected E. coli, taking over the role of GroES, favoring the folding of bacteriophage proteins. Despite being slightly larger, gp31 is quite homologous to GroES in terms of its tertiary and quaternary structure, as well as in its function and mode of interaction with the chaperonin GroEL. Here, we performed a side-by-side comparison of GroES and gp31 heptamer complexes by (ion mobility) tandem mass spectrometry. Surprisingly, we observed quite distinct fragmentation mechanisms for the GroES and gp31 heptamers, whereby GroES displays a unique and unusual bimodal charge distribution in its released monomers. Not only the gas-phase dissociation but also the gas-phase unfolding of GroES and gp31 were found to be very distinct. We rationalize these observations with the similar discrepancies we observed in the thermal unfolding characteristics and surface contacts within GroES and gp31 in the solution. From our data, we propose a model that explains the observed simultaneous dissociation pathways of GroES and the differences between GroES and gp31 gas-phase dissociation and unfolding. We conclude that, although GroES and gp31 exhibit high homology in tertiary and quaternary structure, they are quite distinct in their solution and gas-phase (un)folding characteristics and stability. [Figure: see text] ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1007/s13361-018-1910-5) contains supplementary material, which is available to authorized users. Springer US 2018-05-07 2019 /pmc/articles/PMC6318259/ /pubmed/29736602 http://dx.doi.org/10.1007/s13361-018-1910-5 Text en © The Author(s) 2018 Open Access This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. |
spellingShingle | Focus: Honoring Carol V. Robinson's Election to the National Academy of Sciences: Research Article Dyachenko, Andrey Tamara, Sem Heck, Albert J. R. Distinct Stabilities of the Structurally Homologous Heptameric Co-Chaperonins GroES and gp31 |
title | Distinct Stabilities of the Structurally Homologous Heptameric Co-Chaperonins GroES and gp31 |
title_full | Distinct Stabilities of the Structurally Homologous Heptameric Co-Chaperonins GroES and gp31 |
title_fullStr | Distinct Stabilities of the Structurally Homologous Heptameric Co-Chaperonins GroES and gp31 |
title_full_unstemmed | Distinct Stabilities of the Structurally Homologous Heptameric Co-Chaperonins GroES and gp31 |
title_short | Distinct Stabilities of the Structurally Homologous Heptameric Co-Chaperonins GroES and gp31 |
title_sort | distinct stabilities of the structurally homologous heptameric co-chaperonins groes and gp31 |
topic | Focus: Honoring Carol V. Robinson's Election to the National Academy of Sciences: Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6318259/ https://www.ncbi.nlm.nih.gov/pubmed/29736602 http://dx.doi.org/10.1007/s13361-018-1910-5 |
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