Literature DB >> 22306514

Aggregate reactivation mediated by the Hsp100 chaperones.

Michal Zolkiewski1, Ting Zhang, Maria Nagy.   

Abstract

Hsp100 family of molecular chaperones shows a unique capability to resolubilize and reactivate aggregated proteins. The Hsp100-mediated protein disaggregation is linked to the activity of other chaperones from the Hsp70 and Hsp40 families. The best-studied members of the Hsp100 family are the bacterial ClpB and Hsp104 from yeast. Hsp100 chaperones are members of a large super-family of energy-driven conformational "machines" known as AAA+ ATPases. This review describes the current mechanistic model of the chaperone-induced protein disaggregation and explains how the structural architecture of Hsp100 supports disaggregation and how the co-chaperones may participate in the Hsp100-mediated reactions. Copyright Â
© 2012 Elsevier Inc. All rights reserved.

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Year:  2012        PMID： 22306514      PMCID： PMC3307897          DOI： 10.1016/j.abb.2012.01.012

Source DB:  PubMed          Journal:  Arch Biochem Biophys        ISSN： 0003-9861            Impact factor:   4.013


  88 in total

Review 1.  Posttranslational quality control: folding, refolding, and degrading proteins.

Authors:  S Wickner; M R Maurizi; S Gottesman
Journal:  Science       Date:  1999-12-03       Impact factor: 47.728

2.  Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network.

Authors:  P Goloubinoff; A Mogk; A P Zvi; T Tomoyasu; B Bukau
Journal:  Proc Natl Acad Sci U S A       Date:  1999-11-23       Impact factor: 11.205

3.  Identification of thermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpB.

Authors:  A Mogk; T Tomoyasu; P Goloubinoff; S Rüdiger; D Röder; H Langen; B Bukau
Journal:  EMBO J       Date:  1999-12-15       Impact factor: 11.598

4.  The structures of HsIU and the ATP-dependent protease HsIU-HsIV.

Authors:  M Bochtler; C Hartmann; H K Song; G P Bourenkov; H D Bartunik; R Huber
Journal:  Nature       Date:  2000-02-17       Impact factor: 49.962

5.  Size-dependent disaggregation of stable protein aggregates by the DnaK chaperone machinery.

Authors:  S Diamant; A P Ben-Zvi; B Bukau; P Goloubinoff
Journal:  J Biol Chem       Date:  2000-07-14       Impact factor: 5.157

6.  A novel role for 100 kD heat shock proteins in the parasite Leishmania donovani.

Authors:  S Krobitsch; J Clos
Journal:  Cell Stress Chaperones       Date:  1999-09       Impact factor: 3.667

7.  Microtubule disassembly by ATP-dependent oligomerization of the AAA enzyme katanin.

Authors:  J J Hartman; R D Vale
Journal:  Science       Date:  1999-10-22       Impact factor: 47.728

8.  Heat shock protein 101 plays a crucial role in thermotolerance in Arabidopsis.

Authors:  C Queitsch; S W Hong; E Vierling; S Lindquist
Journal:  Plant Cell       Date:  2000-04       Impact factor: 11.277

9.  Structure and function of the middle domain of ClpB from Escherichia coli.

Authors:  Sabina Kedzierska; Vladimir Akoev; Micheal E Barnett; Michal Zolkiewski
Journal:  Biochemistry       Date:  2003-12-09       Impact factor: 3.162

10.  The mammalian disaggregase machinery: Hsp110 synergizes with Hsp70 and Hsp40 to catalyze protein disaggregation and reactivation in a cell-free system.

Authors:  James Shorter
Journal:  PLoS One       Date:  2011-10-14       Impact factor: 3.240
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  27 in total

Review 1.  Protein rescue from aggregates by powerful molecular chaperone machines.

Authors:  Shannon M Doyle; Olivier Genest; Sue Wickner
Journal:  Nat Rev Mol Cell Biol       Date:  2013-10       Impact factor: 94.444

2.  Hsp104 facilitates the endoplasmic-reticulum-associated degradation of disease-associated and aggregation-prone substrates.

Authors:  Lynley M Doonan; Christopher J Guerriero; G Michael Preston; Teresa M Buck; Netaly Khazanov; Edward A Fisher; Hanoch Senderowitz; Jeffrey L Brodsky
Journal:  Protein Sci       Date:  2019-05-20       Impact factor: 6.725

3.  Interaction between prion protein and Aβ amyloid fibrils revisited.

Authors:  Krzysztof Nieznanski; Krystyna Surewicz; Shugui Chen; Hanna Nieznanska; Witold K Surewicz
Journal:  ACS Chem Neurosci       Date:  2014-04-01       Impact factor: 4.418

4.  Interaction of substrate-mimicking peptides with the AAA+ ATPase ClpB from Escherichia coli.

Authors:  Chathurange B Ranaweera; Przemyslaw Glaza; Taihao Yang; Michal Zolkiewski
Journal:  Arch Biochem Biophys       Date:  2018-08-06       Impact factor: 4.013

5.  Protein aggregation in Ehrlichia chaffeensis during infection of mammalian cells.

Authors:  Dorota Kuczynska-Wisnik; Chuanmin Cheng; Roman R Ganta; Michal Zolkiewski
Journal:  FEMS Microbiol Lett       Date:  2017-03-01       Impact factor: 2.742

6.  Flexible connection of the N-terminal domain in ClpB modulates substrate binding and the aggregate reactivation efficiency.

Authors:  Ting Zhang; Elizabeth A Ploetz; Maria Nagy; Shannon M Doyle; Sue Wickner; Paul E Smith; Michal Zolkiewski
Journal:  Proteins       Date:  2012-09-15

Review 7.  Reactivation of Aggregated Proteins by the ClpB/DnaK Bi-Chaperone System.

Authors:  Michal Zolkiewski; Liudmila S Chesnokova; Stephan N Witt
Journal:  Curr Protoc Protein Sci       Date:  2016-02-02

8.  Physiological response of Pichia pastoris GS115 to methanol-induced high level production of the Hepatitis B surface antigen: catabolic adaptation, stress responses, and autophagic processes.

Authors:  Ana Leticia Vanz; Heinrich Lünsdorf; Ahmad Adnan; Manfred Nimtz; Chandrasekhar Gurramkonda; Navin Khanna; Ursula Rinas
Journal:  Microb Cell Fact       Date:  2012-08-08       Impact factor: 5.328

9.  Aggregate-reactivation activity of the molecular chaperone ClpB from Ehrlichia chaffeensis.

Authors:  Ting Zhang; Sabina Kedzierska-Mieszkowska; Huitao Liu; Chuanmin Cheng; Roman R Ganta; Michal Zolkiewski
Journal:  PLoS One       Date:  2013-05-07       Impact factor: 3.240

10.  Transcription of Ehrlichia chaffeensis genes is accomplished by RNA polymerase holoenzyme containing either sigma 32 or sigma 70.

Authors:  Huitao Liu; Tonia Von Ohlen; Chuanmin Cheng; Bonto Faburay; Roman R Ganta
Journal:  PLoS One       Date:  2013-11-21       Impact factor: 3.240
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