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@article{1491799,
author = {Trčka, Filip and Ďurech, Michal and Vankova, P. and Chmelik, J. and Vandová, Veronika and Hausner, J. and Kadek, A. and Marcoux, J. and Klumpler, Tomáš and Vojtěšek, Bořivoj and Muller, P. and Man, P.},
article_location = {BETHESDA},
article_number = {2},
doi = {http://dx.doi.org/10.1074/mcp.RA118.001044},
keywords = {HEAT-SHOCK-PROTEIN; E3 UBIQUITIN LIGASE; SUBSTRATE-BINDING; CHAPERONE ACTIVITY; MASS-SPECTROMETRY; HYDROGEN/DEUTERIUM EXCHANGE; CONFORMATIONAL DYNAMICS; UNFOLDED PROTEINS; DNAK DIMER; IN-VIVO},
language = {eng},
issn = {1535-9476},
journal = {MOLECULAR & CELLULAR PROTEOMICS},
title = {Human Stress-inducible Hsp70 Has a High Propensity to Form ATP-dependent Antiparallel Dimers That Are Differentially Regulated by Cochaperone Binding},
url = {https://www.mcponline.org/content/18/2/320/tab-article-info},
volume = {18},
year = {2019}
}
TY - JOUR
ID - 1491799
AU - Trčka, Filip - Ďurech, Michal - Vankova, P. - Chmelik, J. - Vandová, Veronika - Hausner, J. - Kadek, A. - Marcoux, J. - Klumpler, Tomáš - Vojtěšek, Bořivoj - Muller, P. - Man, P.
PY - 2019
TI - Human Stress-inducible Hsp70 Has a High Propensity to Form ATP-dependent Antiparallel Dimers That Are Differentially Regulated by Cochaperone Binding
JF - MOLECULAR & CELLULAR PROTEOMICS
VL - 18
IS - 2
SP - 320-337
EP - 320-337
PB - AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
SN - 15359476
KW - HEAT-SHOCK-PROTEIN
KW - E3 UBIQUITIN LIGASE
KW - SUBSTRATE-BINDING
KW - CHAPERONE ACTIVITY
KW - MASS-SPECTROMETRY
KW - HYDROGEN/DEUTERIUM EXCHANGE
KW - CONFORMATIONAL DYNAMICS
KW - UNFOLDED PROTEINS
KW - DNAK DIMER
KW - IN-VIVO
UR - https://www.mcponline.org/content/18/2/320/tab-article-info
L2 - https://www.mcponline.org/content/18/2/320/tab-article-info
N2 - Eukaryotic protein homeostasis (proteostasis) is largely dependent on the action of highly conserved Hsp70 molecular chaperones. Recent evidence indicates that, apart from conserved molecular allostery, Hsp70 proteins have retained and adapted the ability to assemble as functionally relevant ATP-bound dimers throughout evolution. Here, we have compared the ATP-dependent dimerization of DnaK, human stress-inducible Hsp70, Hsc70 and BiP Hsp70 proteins, showing that their dimerization propensities differ, with stress-inducible Hsp70 being predominantly dimeric in the presence of ATP. Structural analyses using hydrogen/deuterium exchange mass spectrometry, native electrospray ionization mass spectrometry and small-angle X-ray scattering revealed that stress-inducible Hsp70 assembles in solution as an antiparallel dimer with the intermolecular interface closely resembling the ATP-bound dimer interfaces captured in DnaK and BiP crystal structures. ATP-dependent dimerization of stress-inducible Hsp70 is necessary for its efficient interaction with Hsp40, as shown by experiments with dimerization-deficient mutants. Moreover, dimerization of ATP-bound Hsp70 is required for its participation in high molecular weight protein complexes detected ex vivo, supporting its functional role in vivo. As human cytosolic Hsp70 can interact with tetratricopeptide repeat (TPR) domain containing cochaperones, we tested the interaction of Hsp70 ATP-dependent dimers with Chip and Tomm34 cochaperones. Although Chip associates with intact Hsp70 dimers to form a larger complex, binding of Tomm34 disrupts the Hsp70 dimer and this event plays an important role in Hsp70 activity regulation. In summary, this study provides structural evidence of robust ATP-dependent antiparallel dimerization of human inducible Hsp70 protein and suggests a novel role of TPR domain cochaperones in multichaperone complexes involving Hsp70 ATP-bound dimers.
ER -
TRČKA, Filip, Michal ĎURECH, P. VANKOVA, J. CHMELIK, Veronika VANDOVÁ, J. HAUSNER, A. KADEK, J. MARCOUX, Tomáš KLUMPLER, Bořivoj VOJTĚŠEK, P. MULLER a P. MAN. Human Stress-inducible Hsp70 Has a High Propensity to Form ATP-dependent Antiparallel Dimers That Are Differentially Regulated by Cochaperone Binding. \textit{MOLECULAR \&{}amp; CELLULAR PROTEOMICS}. BETHESDA: AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC, 2019, roč.~18, č.~2, s.~320-337. ISSN~1535-9476. Dostupné z: https://dx.doi.org/10.1074/mcp.RA118.001044.
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