Nucleotide-Dependent Dimer Association and Dissociation of the Chaperone Hsp90

Katarzyna M. Tych; Markus Jahn; Florian Gegenfurtner; Vera K. Hechtl; Johannes Buchner; Thorsten Hugel; Matthias Rief

doi:10.1021/acs.jpcb.8b07301

Nucleotide-Dependent Dimer Association and Dissociation of the Chaperone Hsp90

Katarzyna M. Tych, Markus Jahn, Florian Gegenfurtner, Vera K. Hechtl, Johannes Buchner, Thorsten Hugel, Matthias Rief^*

^*Corresponding author for this work

Chemical Biology 1

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

9 Citations (Scopus)

Abstract

Hsp90 is an essential molecular chaperone, which has to be in a dimeric form for its correct function. While the affinity of the dimer has previously been measured, little is known about how it associates and dissociates and the factors that influence this. We perform an in-depth single molecule characterization of the C-terminal association and dissociation of Hsp90. We find more than one dissociation rate, indicating that the dimer has a stable and an unstable state. Furthermore, we find that the stability of the C-terminal association is dependent on the presence of ATP, despite the C-terminal dimerization interface being distal to the catalytic site.

Original language	English
Pages (from-to)	11373-11380
Number of pages	8
Journal	Journal of Physical Chemistry B
Volume	122
Issue number	49
DOIs	https://doi.org/10.1021/acs.jpcb.8b07301
Publication status	Published - 13-Dec-2018

Keywords

CONFORMATIONAL DYNAMICS
ATP HYDROLYSIS
PROTEIN
DIMERIZATION
ISOMERIZATION
SPECTROSCOPY
GROWTH
DOMAIN
CPR7

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title = "Nucleotide-Dependent Dimer Association and Dissociation of the Chaperone Hsp90",

abstract = "Hsp90 is an essential molecular chaperone, which has to be in a dimeric form for its correct function. While the affinity of the dimer has previously been measured, little is known about how it associates and dissociates and the factors that influence this. We perform an in-depth single molecule characterization of the C-terminal association and dissociation of Hsp90. We find more than one dissociation rate, indicating that the dimer has a stable and an unstable state. Furthermore, we find that the stability of the C-terminal association is dependent on the presence of ATP, despite the C-terminal dimerization interface being distal to the catalytic site.",

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author = "Tych, {Katarzyna M.} and Markus Jahn and Florian Gegenfurtner and Hechtl, {Vera K.} and Johannes Buchner and Thorsten Hugel and Matthias Rief",

year = "2018",

month = dec,

day = "13",

doi = "10.1021/acs.jpcb.8b07301",

language = "English",

volume = "122",

pages = "11373--11380",

journal = "Journal of Physical Chemistry B",

issn = "1520-6106",

publisher = "AMER CHEMICAL SOC",

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TY - JOUR

T1 - Nucleotide-Dependent Dimer Association and Dissociation of the Chaperone Hsp90

AU - Tych, Katarzyna M.

AU - Jahn, Markus

AU - Gegenfurtner, Florian

AU - Hechtl, Vera K.

AU - Buchner, Johannes

AU - Hugel, Thorsten

AU - Rief, Matthias

PY - 2018/12/13

Y1 - 2018/12/13

N2 - Hsp90 is an essential molecular chaperone, which has to be in a dimeric form for its correct function. While the affinity of the dimer has previously been measured, little is known about how it associates and dissociates and the factors that influence this. We perform an in-depth single molecule characterization of the C-terminal association and dissociation of Hsp90. We find more than one dissociation rate, indicating that the dimer has a stable and an unstable state. Furthermore, we find that the stability of the C-terminal association is dependent on the presence of ATP, despite the C-terminal dimerization interface being distal to the catalytic site.

AB - Hsp90 is an essential molecular chaperone, which has to be in a dimeric form for its correct function. While the affinity of the dimer has previously been measured, little is known about how it associates and dissociates and the factors that influence this. We perform an in-depth single molecule characterization of the C-terminal association and dissociation of Hsp90. We find more than one dissociation rate, indicating that the dimer has a stable and an unstable state. Furthermore, we find that the stability of the C-terminal association is dependent on the presence of ATP, despite the C-terminal dimerization interface being distal to the catalytic site.

KW - CONFORMATIONAL DYNAMICS

KW - ATP HYDROLYSIS

KW - PROTEIN

KW - DIMERIZATION

KW - ISOMERIZATION

KW - SPECTROSCOPY

KW - GROWTH

KW - DOMAIN

KW - CPR7

U2 - 10.1021/acs.jpcb.8b07301

DO - 10.1021/acs.jpcb.8b07301

M3 - Article

SN - 1520-6106

VL - 122

SP - 11373

EP - 11380

JO - Journal of Physical Chemistry B

JF - Journal of Physical Chemistry B

IS - 49

ER -

Nucleotide-Dependent Dimer Association and Dissociation of the Chaperone Hsp90

Abstract

Keywords

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