Literature DB >> 20519287

A more precise characterization of chaperonin substrates.

Emanuele Raineri1, Paolo Ribeca, Luis Serrano, Tobias Maier.   

Abstract

MOTIVATION: Molecular chaperones prevent the aggregation of their substrate proteins and thereby ensure that they reach their functional native state. The bacterial GroEL/ES chaperonin system is understood in great detail on a structural, mechanistic and functional level; its interactors in Escherichia coli have been identified and characterized. However, a long-standing question in the field is: What makes a protein a chaperone substrate?
RESULTS: Here we identify, using a bioinformatics-based approach a simple set of quantities, which characterize the GroEL-substrate proteome. We define three novel parameters differentiating GroEL interactors from other cellular proteins: lower rate of evolution, hydrophobicity and aggregation propensity. Combining them with other known features to a simple Bayesian predictor allows us to identify known homologous and heterologous GroEL substrateproteins. We discuss our findings in relation to established mechanisms of protein folding and evolutionary buffering by chaperones.

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Year:  2010        PMID: 20519287     DOI: 10.1093/bioinformatics/btq287

Source DB:  PubMed          Journal:  Bioinformatics        ISSN: 1367-4803            Impact factor:   6.937


  13 in total

1.  Indole-3-glycerol-phosphate synthase is recognized by a cold-inducible group II chaperonin in Thermococcus kodakarensis.

Authors:  Le Gao; Atsushi Danno; Sayaka Fujii; Wakao Fukuda; Tadayuki Imanaka; Shinsuke Fujiwara
Journal:  Appl Environ Microbiol       Date:  2012-03-23       Impact factor: 4.792

Review 2.  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

3.  Identification of a novel protein binding motif within the T-synthase for the molecular chaperone Cosmc.

Authors:  Rajindra P Aryal; Tongzhong Ju; Richard D Cummings
Journal:  J Biol Chem       Date:  2014-03-10       Impact factor: 5.157

4.  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

5.  T3SEdb: data warehousing of virulence effectors secreted by the bacterial Type III Secretion System.

Authors:  Daniel Ming Ming Tay; Kunde Ramamoorthy Govindarajan; Asif M Khan; Terenze Yao Rui Ong; Hanif M Samad; Wei Wei Soh; Minyan Tong; Fan Zhang; Tin Wee Tan
Journal:  BMC Bioinformatics       Date:  2010-10-15       Impact factor: 3.169

6.  Difference in the distribution pattern of substrate enzymes in the metabolic network of Escherichia coli, according to chaperonin requirement.

Authors:  Kazuhiro Takemoto; Tatsuya Niwa; Hideki Taguchi
Journal:  BMC Syst Biol       Date:  2011-06-24

7.  Reduced selective constraint in endosymbionts: elevation in radical amino acid replacements occurs genome-wide.

Authors:  Jennifer J Wernegreen
Journal:  PLoS One       Date:  2011-12-14       Impact factor: 3.240

8.  Decoding Structural Properties of a Partially Unfolded Protein Substrate: En Route to Chaperone Binding.

Authors:  Suhani Nagpal; Satyam Tiwari; Koyeli Mapa; Lipi Thukral
Journal:  PLoS Comput Biol       Date:  2015-09-22       Impact factor: 4.475

9.  How do eubacterial organisms manage aggregation-prone proteome?

Authors:  Rishi Das Roy; Manju Bhardwaj; Vasudha Bhatnagar; Kausik Chakraborty; Debasis Dash
Journal:  F1000Res       Date:  2014-06-27

10.  Interplay between chaperones and protein disorder promotes the evolution of protein networks.

Authors:  Sebastian Pechmann; Judith Frydman
Journal:  PLoS Comput Biol       Date:  2014-06-26       Impact factor: 4.475

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