Literature DB >> 20416322

Physicochemical determinants of chaperone requirements.

Gian Gaetano Tartaglia1, Christopher M Dobson, F Ulrich Hartl, Michele Vendruscolo.   

Abstract

We describe a series of stringent relationships between abundance, solubility and chaperone usage of proteins. Based on these relationships, we show that the need of Escherichia coli proteins for the chaperonin GroEL can be predicted with 86% accuracy. Furthermore, from the observation that the abundance and solubility of proteins depend on the physicochemical properties of their amino acid sequences, we demonstrate that the requirement for GroEL can also be predicted directly from the sequences with 90% accuracy. These results indicate that the physicochemical properties of the amino acid sequences represent an essential component of the cellular quality control system that ensures the maintenance of protein homeostasis in living systems. 2010. Published by Elsevier Ltd.

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Year:  2010        PMID: 20416322     DOI: 10.1016/j.jmb.2010.03.066

Source DB:  PubMed          Journal:  J Mol Biol        ISSN: 0022-2836            Impact factor:   5.469


  25 in total

Review 1.  Molecular chaperones in protein folding and proteostasis.

Authors:  F Ulrich Hartl; Andreas Bracher; Manajit Hayer-Hartl
Journal:  Nature       Date:  2011-07-20       Impact factor: 49.962

2.  Structural analysis of SARS-CoV-2 genome and predictions of the human interactome.

Authors:  Andrea Vandelli; Michele Monti; Edoardo Milanetti; Alexandros Armaos; Jakob Rupert; Elsa Zacco; Elias Bechara; Riccardo Delli Ponti; Gian Gaetano Tartaglia
Journal:  Nucleic Acids Res       Date:  2020-11-18       Impact factor: 16.971

3.  Crowding activates ClpB and enhances its association with DnaK for efficient protein aggregate reactivation.

Authors:  Ianire Martín; Garbiñe Celaya; Carlos Alfonso; Fernando Moro; Germán Rivas; Arturo Muga
Journal:  Biophys J       Date:  2014-05-06       Impact factor: 4.033

4.  Group II archaeal chaperonin recognition of partially folded human γD-crystallin mutants.

Authors:  Oksana A Sergeeva; Jingkun Yang; Jonathan A King; Kelly M Knee
Journal:  Protein Sci       Date:  2014-04-05       Impact factor: 6.725

5.  Local energetic frustration affects the dependence of green fluorescent protein folding on the chaperonin GroEL.

Authors:  Boudhayan Bandyopadhyay; Adi Goldenzweig; Tamar Unger; Orit Adato; Sarel J Fleishman; Ron Unger; Amnon Horovitz
Journal:  J Biol Chem       Date:  2017-10-24       Impact factor: 5.157

6.  Pervasive convergent evolution and extreme phenotypes define chaperone requirements of protein homeostasis.

Authors:  Yasmine Draceni; Sebastian Pechmann
Journal:  Proc Natl Acad Sci U S A       Date:  2019-09-16       Impact factor: 11.205

7.  Global analysis of chaperone effects using a reconstituted cell-free translation system.

Authors:  Tatsuya Niwa; Takashi Kanamori; Takuya Ueda; Hideki Taguchi
Journal:  Proc Natl Acad Sci U S A       Date:  2012-05-21       Impact factor: 11.205

8.  The cotranslational function of ribosome-associated Hsp70 in eukaryotic protein homeostasis.

Authors:  Felix Willmund; Marta del Alamo; Sebastian Pechmann; Taotao Chen; Véronique Albanèse; Eric B Dammer; Junmin Peng; Judith Frydman
Journal:  Cell       Date:  2013-01-17       Impact factor: 41.582

Review 9.  The ribosome as a hub for protein quality control.

Authors:  Sebastian Pechmann; Felix Willmund; Judith Frydman
Journal:  Mol Cell       Date:  2013-02-07       Impact factor: 17.970

10.  Conversion of a chaperonin GroEL-independent protein into an obligate substrate.

Authors:  Takuya Ishimoto; Kei Fujiwara; Tatsuya Niwa; Hideki Taguchi
Journal:  J Biol Chem       Date:  2014-10-06       Impact factor: 5.157

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