Literature DB >> 18702035

Role of the ribosome in protein folding.

Debasis Das1, Anindita Das, Dibyendu Samanta, Jaydip Ghosh, Santanu Dasgupta, Arpita Bhattacharya, Arunima Basu, Suparna Sanyal, Chanchal Das Gupta.   

Abstract

In all organisms, the ribosome synthesizes and folds full length polypeptide chains into active three-dimensional conformations. The nascent protein goes through two major interactions, first with the ribosome which synthesizes the polypeptide chain and holds it for a considerable length of time, and then with the chaperones. Some of the chaperones are found in solution as well as associated to the ribosome. A number of in vitro and in vivo experiments revealed that the nascent protein folds through specific interactions of some amino acids with the nucleotides in the peptidyl transferase center (PTC) in the large ribosomal subunit. The mechanism of this folding differs from self-folding. In this article, we highlight the folding of nascent proteins on the ribosome and the influence of chaperones etc. on protein folding.

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Year:  2008        PMID: 18702035     DOI: 10.1002/biot.200800098

Source DB:  PubMed          Journal:  Biotechnol J        ISSN: 1860-6768            Impact factor:   4.677


  22 in total

1.  Involvement of mitochondrial ribosomal proteins in ribosomal RNA-mediated protein folding.

Authors:  Anindita Das; Jaydip Ghosh; Arpita Bhattacharya; Dibyendu Samanta; Debasis Das; Chanchal Das Gupta
Journal:  J Biol Chem       Date:  2011-10-21       Impact factor: 5.157

Review 2.  Protein folding and aggregation in bacteria.

Authors:  Raimon Sabate; Natalia S de Groot; Salvador Ventura
Journal:  Cell Mol Life Sci       Date:  2010-04-01       Impact factor: 9.261

3.  Distinct modulatory role of RNA in the aggregation of the tumor suppressor protein p53 core domain.

Authors:  Petar Stefanov Kovachev; Debapriya Banerjee; Luciana Pereira Rangel; Jonny Eriksson; Murilo M Pedrote; Mafalda Maria D C Martins-Dinis; Katarina Edwards; Yraima Cordeiro; Jerson L Silva; Suparna Sanyal
Journal:  J Biol Chem       Date:  2017-04-18       Impact factor: 5.157

4.  Prion 2016 Oral Abstracts.

Authors: 
Journal:  Prion       Date:  2016       Impact factor: 3.931

Review 5.  The double life of the ribosome: When its protein folding activity supports prion propagation.

Authors:  Cécile Voisset; Marc Blondel; Gary W Jones; Gaëlle Friocourt; Guillaume Stahl; Stéphane Chédin; Vincent Béringue; Reynald Gillet
Journal:  Prion       Date:  2017-03-04       Impact factor: 3.931

Review 6.  Unraveling co-translational protein folding: Concepts and methods.

Authors:  Anton A Komar
Journal:  Methods       Date:  2017-12-06       Impact factor: 3.608

7.  Development of high-yield autofluorescent protein microarrays using hybrid cell-free expression with combined Escherichia coli S30 and wheat germ extracts.

Authors:  Xristo Zárate; David C Henderson; Keenan C Phillips; April D Lake; David W Galbraith
Journal:  Proteome Sci       Date:  2010-06-15       Impact factor: 2.480

8.  The antiprion compound 6-aminophenanthridine inhibits the protein folding activity of the ribosome by direct competition.

Authors:  Yanhong Pang; Sriram Kurella; Cécile Voisset; Dibyendu Samanta; Debapriya Banerjee; Ariane Schabe; Chanchal Das Gupta; Hervé Galons; Marc Blondel; Suparna Sanyal
Journal:  J Biol Chem       Date:  2013-05-14       Impact factor: 5.157

9.  Anti-prion Drugs Targeting the Protein Folding Activity of the Ribosome Reduce PABPN1 Aggregation.

Authors:  Aline Bamia; Maha Sinane; Rima Naït-Saïdi; Jamila Dhiab; Frédéric Bihel; Cécile Voisset; Marc Keruzoré; Phu Hai Nguyen; Agathe Bertho; Flavie Soubigou; Sophie Halliez; Marc Blondel; Capucine Trollet; Martine Simonelig; Gaëlle Friocourt; Vincent Béringue
Journal:  Neurotherapeutics       Date:  2021-02-02       Impact factor: 7.620

Review 10.  A Conceptual Framework for Integrating Cellular Protein Folding, Misfolding and Aggregation.

Authors:  Seong Il Choi; Baik L Seong
Journal:  Life (Basel)       Date:  2021-06-24
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