Probing the folding-unfolding transition of a thermophilic protein, MTH1880

Heeyoun Kim; Sangyeol Kim; Youngjin Jung; Jeongmin Han; Ji Hye Yun; Iksoo Chang; Weontae Lee

doi:10.1371/journal.pone.0145853

Probing the folding-unfolding transition of a thermophilic protein, MTH1880

Heeyoun Kim, Sangyeol Kim, Youngjin Jung, Jeongmin Han, Ji Hye Yun, Iksoo Chang, Weontae Lee

Research output: Contribution to journal › Article › peer-review

2 Citations (Scopus)

Abstract

The folding mechanism of typical proteins has been studied widely, while our understanding of the origin of the high stability of thermophilic proteins is still elusive. Of particular interest is how an atypical thermophilic protein with a novel fold maintains its structure and stability under extreme conditions. Folding-unfolding transitions of MTH1880, a thermophilic protein from Methanobacterium thermoautotrophicum, induced by heat, urea, and GdnHCl, were investigated using spectroscopic techniques including circular dichorism, fluorescence, NMR combined with molecular dynamics (MD) simulations. Our results suggest that MTH1880 undergoes a two-state N to D transition and it is extremely stable against temperature and denaturants. The reversibility of refolding was confirmed by spectroscopic methods and size exclusion chromatography. We found that the hyper-stability of the thermophilic MTH1880 protein originates from an extensive network of both electrostatic and hydrophobic interactions coordinated by the central β-sheet. Spectroscopic measurements, in combination with computational simulations, have helped to clarify the thermodynamic and structural basis for hyper-stability of the novel thermophilic protein MTH1880.

Original language	English
Article number	e0145853
Journal	PloS one
Volume	11
Issue number	1
DOIs	https://doi.org/10.1371/journal.pone.0145853
Publication status	Published - 2016 Jan 1

Bibliographical note

Funding Information:
This work was funded by the Ministry of Future Creation and Science (MFCS) of Korea, the Translational Research Center for Protein Function Control (2009-0083522), and the Mid-career Researcher Program (2012-010285). HK, YJ and JH were supported by a BK21plus program from the MFCS. It was also supported by the Creative Research Initiatives (Center for Proteome Biophysics) of National Research Foundation, Korea (No. 2008-0061984 to SK and IC), and MIREBraiN program (I. C: No. 2015010013) from Daegu Gyeongbuk Institute of Science and Technology. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript. This work was funded by the Ministry of Future Creation and Science (MFCS) of Korea, the Translational Research Center for Protein Function Control (2009-0083522), and the Midcareer Researcher Program (2012-010285). HK, YJ, JY and JH were supported by a BK21plus program from the MFCS. It was also supported by the Creative Research Initiatives (Center for Proteome Biophysics) of National Research Foundation, Korea (No. 2008-0061984 to S.K, and I.C) and MIREBraiN program (I.C: No. 2015010013) from DGIST.

Publisher Copyright:
© 2016 Kim et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

All Science Journal Classification (ASJC) codes

Biochemistry, Genetics and Molecular Biology(all)
Agricultural and Biological Sciences(all)
General

Access to Document

10.1371/journal.pone.0145853

Fingerprint Dive into the research topics of 'Probing the folding-unfolding transition of a thermophilic protein, MTH1880'. Together they form a unique fingerprint.

Cite this

@article{2e946db65e014934af4c966275d945e4,

title = "Probing the folding-unfolding transition of a thermophilic protein, MTH1880",

abstract = "The folding mechanism of typical proteins has been studied widely, while our understanding of the origin of the high stability of thermophilic proteins is still elusive. Of particular interest is how an atypical thermophilic protein with a novel fold maintains its structure and stability under extreme conditions. Folding-unfolding transitions of MTH1880, a thermophilic protein from Methanobacterium thermoautotrophicum, induced by heat, urea, and GdnHCl, were investigated using spectroscopic techniques including circular dichorism, fluorescence, NMR combined with molecular dynamics (MD) simulations. Our results suggest that MTH1880 undergoes a two-state N to D transition and it is extremely stable against temperature and denaturants. The reversibility of refolding was confirmed by spectroscopic methods and size exclusion chromatography. We found that the hyper-stability of the thermophilic MTH1880 protein originates from an extensive network of both electrostatic and hydrophobic interactions coordinated by the central β-sheet. Spectroscopic measurements, in combination with computational simulations, have helped to clarify the thermodynamic and structural basis for hyper-stability of the novel thermophilic protein MTH1880.",

author = "Heeyoun Kim and Sangyeol Kim and Youngjin Jung and Jeongmin Han and Yun, {Ji Hye} and Iksoo Chang and Weontae Lee",

note = "Funding Information: This work was funded by the Ministry of Future Creation and Science (MFCS) of Korea, the Translational Research Center for Protein Function Control (2009-0083522), and the Mid-career Researcher Program (2012-010285). HK, YJ and JH were supported by a BK21plus program from the MFCS. It was also supported by the Creative Research Initiatives (Center for Proteome Biophysics) of National Research Foundation, Korea (No. 2008-0061984 to SK and IC), and MIREBraiN program (I. C: No. 2015010013) from Daegu Gyeongbuk Institute of Science and Technology. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript. This work was funded by the Ministry of Future Creation and Science (MFCS) of Korea, the Translational Research Center for Protein Function Control (2009-0083522), and the Midcareer Researcher Program (2012-010285). HK, YJ, JY and JH were supported by a BK21plus program from the MFCS. It was also supported by the Creative Research Initiatives (Center for Proteome Biophysics) of National Research Foundation, Korea (No. 2008-0061984 to S.K, and I.C) and MIREBraiN program (I.C: No. 2015010013) from DGIST. Publisher Copyright: {\textcopyright} 2016 Kim et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.",

year = "2016",

month = jan,

day = "1",

doi = "10.1371/journal.pone.0145853",

language = "English",

volume = "11",

journal = "PLoS One",

issn = "1932-6203",

publisher = "Public Library of Science",

number = "1",

}

TY - JOUR

T1 - Probing the folding-unfolding transition of a thermophilic protein, MTH1880

AU - Kim, Heeyoun

AU - Kim, Sangyeol

AU - Jung, Youngjin

AU - Han, Jeongmin

AU - Yun, Ji Hye

AU - Chang, Iksoo

AU - Lee, Weontae

N1 - Funding Information: This work was funded by the Ministry of Future Creation and Science (MFCS) of Korea, the Translational Research Center for Protein Function Control (2009-0083522), and the Mid-career Researcher Program (2012-010285). HK, YJ and JH were supported by a BK21plus program from the MFCS. It was also supported by the Creative Research Initiatives (Center for Proteome Biophysics) of National Research Foundation, Korea (No. 2008-0061984 to SK and IC), and MIREBraiN program (I. C: No. 2015010013) from Daegu Gyeongbuk Institute of Science and Technology. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript. This work was funded by the Ministry of Future Creation and Science (MFCS) of Korea, the Translational Research Center for Protein Function Control (2009-0083522), and the Midcareer Researcher Program (2012-010285). HK, YJ, JY and JH were supported by a BK21plus program from the MFCS. It was also supported by the Creative Research Initiatives (Center for Proteome Biophysics) of National Research Foundation, Korea (No. 2008-0061984 to S.K, and I.C) and MIREBraiN program (I.C: No. 2015010013) from DGIST. Publisher Copyright: © 2016 Kim et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

PY - 2016/1/1

Y1 - 2016/1/1

N2 - The folding mechanism of typical proteins has been studied widely, while our understanding of the origin of the high stability of thermophilic proteins is still elusive. Of particular interest is how an atypical thermophilic protein with a novel fold maintains its structure and stability under extreme conditions. Folding-unfolding transitions of MTH1880, a thermophilic protein from Methanobacterium thermoautotrophicum, induced by heat, urea, and GdnHCl, were investigated using spectroscopic techniques including circular dichorism, fluorescence, NMR combined with molecular dynamics (MD) simulations. Our results suggest that MTH1880 undergoes a two-state N to D transition and it is extremely stable against temperature and denaturants. The reversibility of refolding was confirmed by spectroscopic methods and size exclusion chromatography. We found that the hyper-stability of the thermophilic MTH1880 protein originates from an extensive network of both electrostatic and hydrophobic interactions coordinated by the central β-sheet. Spectroscopic measurements, in combination with computational simulations, have helped to clarify the thermodynamic and structural basis for hyper-stability of the novel thermophilic protein MTH1880.

AB - The folding mechanism of typical proteins has been studied widely, while our understanding of the origin of the high stability of thermophilic proteins is still elusive. Of particular interest is how an atypical thermophilic protein with a novel fold maintains its structure and stability under extreme conditions. Folding-unfolding transitions of MTH1880, a thermophilic protein from Methanobacterium thermoautotrophicum, induced by heat, urea, and GdnHCl, were investigated using spectroscopic techniques including circular dichorism, fluorescence, NMR combined with molecular dynamics (MD) simulations. Our results suggest that MTH1880 undergoes a two-state N to D transition and it is extremely stable against temperature and denaturants. The reversibility of refolding was confirmed by spectroscopic methods and size exclusion chromatography. We found that the hyper-stability of the thermophilic MTH1880 protein originates from an extensive network of both electrostatic and hydrophobic interactions coordinated by the central β-sheet. Spectroscopic measurements, in combination with computational simulations, have helped to clarify the thermodynamic and structural basis for hyper-stability of the novel thermophilic protein MTH1880.

UR - http://www.scopus.com/inward/record.url?scp=84955481706&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84955481706&partnerID=8YFLogxK

U2 - 10.1371/journal.pone.0145853

DO - 10.1371/journal.pone.0145853

M3 - Article

C2 - 26766214

AN - SCOPUS:84955481706

VL - 11

JO - PLoS One

JF - PLoS One

SN - 1932-6203

IS - 1

M1 - e0145853

ER -

Probing the folding-unfolding transition of a thermophilic protein, MTH1880

Abstract

Bibliographical note

All Science Journal Classification (ASJC) codes

Access to Document

Other files and links

Cite this