Publication

Folding and Domain Interactions of Three Orthologs of Hsp90 Studied by Single-Molecule Force Spectroscopy

Jahn, M., Tych, K., Girstmair, H., Steinmaßl, M., Hugel, T., Buchner, J. & Rief, M., 2-Jan-2018, In : Structure. 26, 1, p. 96-105.e4

Research output: Contribution to journalArticleAcademicpeer-review

APA

Jahn, M., Tych, K., Girstmair, H., Steinmaßl, M., Hugel, T., Buchner, J., & Rief, M. (2018). Folding and Domain Interactions of Three Orthologs of Hsp90 Studied by Single-Molecule Force Spectroscopy. Structure, 26(1), 96-105.e4. https://doi.org/10.1016/j.str.2017.11.023

Author

Jahn, Markus ; Tych, Katarzyna ; Girstmair, Hannah ; Steinmaßl, Maximilian ; Hugel, Thorsten ; Buchner, Johannes ; Rief, Matthias. / Folding and Domain Interactions of Three Orthologs of Hsp90 Studied by Single-Molecule Force Spectroscopy. In: Structure. 2018 ; Vol. 26, No. 1. pp. 96-105.e4.

Harvard

Jahn, M, Tych, K, Girstmair, H, Steinmaßl, M, Hugel, T, Buchner, J & Rief, M 2018, 'Folding and Domain Interactions of Three Orthologs of Hsp90 Studied by Single-Molecule Force Spectroscopy', Structure, vol. 26, no. 1, pp. 96-105.e4. https://doi.org/10.1016/j.str.2017.11.023

Standard

Folding and Domain Interactions of Three Orthologs of Hsp90 Studied by Single-Molecule Force Spectroscopy. / Jahn, Markus; Tych, Katarzyna; Girstmair, Hannah; Steinmaßl, Maximilian; Hugel, Thorsten; Buchner, Johannes; Rief, Matthias.

In: Structure, Vol. 26, No. 1, 02.01.2018, p. 96-105.e4.

Research output: Contribution to journalArticleAcademicpeer-review

Vancouver

Jahn M, Tych K, Girstmair H, Steinmaßl M, Hugel T, Buchner J et al. Folding and Domain Interactions of Three Orthologs of Hsp90 Studied by Single-Molecule Force Spectroscopy. Structure. 2018 Jan 2;26(1):96-105.e4. https://doi.org/10.1016/j.str.2017.11.023


BibTeX

@article{b64f3dc6ff4540c4921f01a6dba13774,
title = "Folding and Domain Interactions of Three Orthologs of Hsp90 Studied by Single-Molecule Force Spectroscopy",
abstract = "The heat-shock protein 90 (Hsp90) molecular chaperones are highly conserved across species. However, their dynamic properties can vary significantly from organism to organism. Here we used high-precision optical tweezers to analyze the mechanical properties and folding of different Hsp90 orthologs, namely bacterial Hsp90 (HtpG) and Hsp90 from the endoplasmic reticulum (ER) (Grp94), as well as from the cytosol of the eukaryotic cell (Hsp82). We find that the folding rates of Hsp82 and HtpG are similar, while the folding of Grp94 is slowed down by misfolding of the N-terminal domain. Furthermore, the domain interactions mediated by the charged linker, involved in the conformational cycles of all three orthologs, are much stronger for Grp94 than for Hsp82, keeping the N-terminal domain and the middle domain in close proximity. Thus, the ER resident Hsp90 ortholog differs from the cytosolic counterparts in basic functionally relevant structural properties. Jahn and Tych et al. report high-precision optical tweezers experiments to analyze the structural and mechanical properties of three orthologs of the heat-shock protein 90 (Hsp90) molecular chaperone family. Hsp90s are highly conserved across species. They find differences in folding rates, domain interactions, and functionally relevant structural stabilities.",
keywords = "chaperones, conformational dynamics, heat-shock protein 90, optical tweezers, protein folding, single molecule",
author = "Markus Jahn and Katarzyna Tych and Hannah Girstmair and Maximilian Steinma{\ss}l and Thorsten Hugel and Johannes Buchner and Matthias Rief",
year = "2018",
month = jan,
day = "2",
doi = "10.1016/j.str.2017.11.023",
language = "English",
volume = "26",
pages = "96--105.e4",
journal = "Structure",
issn = "1878-4186",
publisher = "CELL PRESS",
number = "1",

}

RIS

TY - JOUR

T1 - Folding and Domain Interactions of Three Orthologs of Hsp90 Studied by Single-Molecule Force Spectroscopy

AU - Jahn, Markus

AU - Tych, Katarzyna

AU - Girstmair, Hannah

AU - Steinmaßl, Maximilian

AU - Hugel, Thorsten

AU - Buchner, Johannes

AU - Rief, Matthias

PY - 2018/1/2

Y1 - 2018/1/2

N2 - The heat-shock protein 90 (Hsp90) molecular chaperones are highly conserved across species. However, their dynamic properties can vary significantly from organism to organism. Here we used high-precision optical tweezers to analyze the mechanical properties and folding of different Hsp90 orthologs, namely bacterial Hsp90 (HtpG) and Hsp90 from the endoplasmic reticulum (ER) (Grp94), as well as from the cytosol of the eukaryotic cell (Hsp82). We find that the folding rates of Hsp82 and HtpG are similar, while the folding of Grp94 is slowed down by misfolding of the N-terminal domain. Furthermore, the domain interactions mediated by the charged linker, involved in the conformational cycles of all three orthologs, are much stronger for Grp94 than for Hsp82, keeping the N-terminal domain and the middle domain in close proximity. Thus, the ER resident Hsp90 ortholog differs from the cytosolic counterparts in basic functionally relevant structural properties. Jahn and Tych et al. report high-precision optical tweezers experiments to analyze the structural and mechanical properties of three orthologs of the heat-shock protein 90 (Hsp90) molecular chaperone family. Hsp90s are highly conserved across species. They find differences in folding rates, domain interactions, and functionally relevant structural stabilities.

AB - The heat-shock protein 90 (Hsp90) molecular chaperones are highly conserved across species. However, their dynamic properties can vary significantly from organism to organism. Here we used high-precision optical tweezers to analyze the mechanical properties and folding of different Hsp90 orthologs, namely bacterial Hsp90 (HtpG) and Hsp90 from the endoplasmic reticulum (ER) (Grp94), as well as from the cytosol of the eukaryotic cell (Hsp82). We find that the folding rates of Hsp82 and HtpG are similar, while the folding of Grp94 is slowed down by misfolding of the N-terminal domain. Furthermore, the domain interactions mediated by the charged linker, involved in the conformational cycles of all three orthologs, are much stronger for Grp94 than for Hsp82, keeping the N-terminal domain and the middle domain in close proximity. Thus, the ER resident Hsp90 ortholog differs from the cytosolic counterparts in basic functionally relevant structural properties. Jahn and Tych et al. report high-precision optical tweezers experiments to analyze the structural and mechanical properties of three orthologs of the heat-shock protein 90 (Hsp90) molecular chaperone family. Hsp90s are highly conserved across species. They find differences in folding rates, domain interactions, and functionally relevant structural stabilities.

KW - chaperones

KW - conformational dynamics

KW - heat-shock protein 90

KW - optical tweezers

KW - protein folding

KW - single molecule

UR - http://www.scopus.com/inward/record.url?scp=85038872357&partnerID=8YFLogxK

U2 - 10.1016/j.str.2017.11.023

DO - 10.1016/j.str.2017.11.023

M3 - Article

C2 - 29276035

AN - SCOPUS:85038872357

VL - 26

SP - 96-105.e4

JO - Structure

JF - Structure

SN - 1878-4186

IS - 1

ER -

ID: 124556627