In vitro protein folding by E. coli ribosome: Unfolded protein splitting 70S to interact with 50S subunit

Arunima Basu; Dibyendu Samanta; Debasis Das; Saheli Chowdhury; Arpita Bhattacharya; Jaydip Ghosh; Anindita Das; Chanchal DasGupta

doi:10.1016/j.bbrc.2007.11.143

In vitro protein folding by E. coli ribosome: Unfolded protein splitting 70S to interact with 50S subunit

Arunima Basu, Dibyendu Samanta, Debasis Das, Saheli Chowdhury, Arpita Bhattacharya, Jaydip Ghosh, Anindita Das, Chanchal DasGupta

Research output: Contribution to journal › Article › peer-review

24 Scopus citations

Abstract

Folding of unfolded protein on Escherichia coli 70S ribosome is accompanied by rapid dissociation of the ribosome into 50S and 30S subunits. The dissociation rate of 70S ribosome with unfolded protein is much faster than that caused by combined effect of translation and polypeptide release factors known to be involved in the dissociation of ribosome into subunits. The protein then reaches a "folding competent" state on 50S and is released to take up native conformation by itself. Release before attaining the folding competent state or prevention of release by cross-linking it with ribosome, would not allow the protein to get back to its native conformation.

Original language	English (US)
Pages (from-to)	598-603
Number of pages	6
Journal	Biochemical and Biophysical Research Communications
Volume	366
Issue number	2
DOIs	https://doi.org/10.1016/j.bbrc.2007.11.143
State	Published - Feb 8 2008
Externally published	Yes

Keywords

50S subunit
Protein folding
Ribosomal subunit dissociation

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

Access to Document

10.1016/j.bbrc.2007.11.143

Cite this

@article{2a5dc71bac8144bf8dc2d9697369c8be,

title = "In vitro protein folding by E. coli ribosome: Unfolded protein splitting 70S to interact with 50S subunit",

abstract = "Folding of unfolded protein on Escherichia coli 70S ribosome is accompanied by rapid dissociation of the ribosome into 50S and 30S subunits. The dissociation rate of 70S ribosome with unfolded protein is much faster than that caused by combined effect of translation and polypeptide release factors known to be involved in the dissociation of ribosome into subunits. The protein then reaches a {"}folding competent{"} state on 50S and is released to take up native conformation by itself. Release before attaining the folding competent state or prevention of release by cross-linking it with ribosome, would not allow the protein to get back to its native conformation.",

keywords = "50S subunit, Protein folding, Ribosomal subunit dissociation",

author = "Arunima Basu and Dibyendu Samanta and Debasis Das and Saheli Chowdhury and Arpita Bhattacharya and Jaydip Ghosh and Anindita Das and Chanchal DasGupta",

note = "Funding Information: We thank Prof. U. Vershney, Indian Institute of Science, Bangalore, for providing EFG, RRF and IF3 clones. The consistent help from Prof. D.K. Chattoraj, NIH, USA at various stages of the work is gratefully acknowledged. The research was supported by grants from DBT, CSIR, FIST, UGC-DSA. ",

year = "2008",

month = feb,

day = "8",

doi = "10.1016/j.bbrc.2007.11.143",

language = "English (US)",

volume = "366",

pages = "598--603",

journal = "Biochemical and Biophysical Research Communications",

issn = "0006-291X",

publisher = "Academic Press Inc.",

number = "2",

}

TY - JOUR

T1 - In vitro protein folding by E. coli ribosome

T2 - Unfolded protein splitting 70S to interact with 50S subunit

AU - Basu, Arunima

AU - Samanta, Dibyendu

AU - Das, Debasis

AU - Chowdhury, Saheli

AU - Bhattacharya, Arpita

AU - Ghosh, Jaydip

AU - Das, Anindita

AU - DasGupta, Chanchal

N1 - Funding Information: We thank Prof. U. Vershney, Indian Institute of Science, Bangalore, for providing EFG, RRF and IF3 clones. The consistent help from Prof. D.K. Chattoraj, NIH, USA at various stages of the work is gratefully acknowledged. The research was supported by grants from DBT, CSIR, FIST, UGC-DSA.

PY - 2008/2/8

Y1 - 2008/2/8

N2 - Folding of unfolded protein on Escherichia coli 70S ribosome is accompanied by rapid dissociation of the ribosome into 50S and 30S subunits. The dissociation rate of 70S ribosome with unfolded protein is much faster than that caused by combined effect of translation and polypeptide release factors known to be involved in the dissociation of ribosome into subunits. The protein then reaches a "folding competent" state on 50S and is released to take up native conformation by itself. Release before attaining the folding competent state or prevention of release by cross-linking it with ribosome, would not allow the protein to get back to its native conformation.

AB - Folding of unfolded protein on Escherichia coli 70S ribosome is accompanied by rapid dissociation of the ribosome into 50S and 30S subunits. The dissociation rate of 70S ribosome with unfolded protein is much faster than that caused by combined effect of translation and polypeptide release factors known to be involved in the dissociation of ribosome into subunits. The protein then reaches a "folding competent" state on 50S and is released to take up native conformation by itself. Release before attaining the folding competent state or prevention of release by cross-linking it with ribosome, would not allow the protein to get back to its native conformation.

KW - 50S subunit

KW - Protein folding

KW - Ribosomal subunit dissociation

UR - http://www.scopus.com/inward/record.url?scp=37449003019&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=37449003019&partnerID=8YFLogxK

U2 - 10.1016/j.bbrc.2007.11.143

DO - 10.1016/j.bbrc.2007.11.143

M3 - Article

C2 - 18068121

AN - SCOPUS:37449003019

SN - 0006-291X

VL - 366

SP - 598

EP - 603

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 2

ER -

In vitro protein folding by E. coli ribosome: Unfolded protein splitting 70S to interact with 50S subunit

Abstract

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this