Open Access

Molecular Microbiology

The conformation of a nascent polypeptide inside the ribosome tunnel affects protein targeting and protein folding

Peterson J.H., Woolhead C.A., Bernstein H.D.

Publication type: Journal Article

Publication date: 2010-08-20

Wiley

Journal: Molecular Microbiology

Quartile SCImago

Quartile WOS

Impact factor: 3.6

ISSN: 0950382X, 13652958

DOI: 10.1111/j.1365-2958.2010.07325.x

Copy DOI

PubMed ID: 20804452

Abstract

In this report, we describe insights into the function of the ribosome tunnel that were obtained through an analysis of an unusual 25 residue N‐terminal motif (EspP1‐25) associated with the signal peptide of the Escherichia coli EspP protein. It was previously shown that EspP1‐25 inhibits signal peptide recognition by the signal recognition particle, and we now show that fusion of EspP1‐25 to a cytoplasmic protein causes it to aggregate. We obtained two lines of evidence that both of these effects are attributable to the conformation of EspP1‐25 inside the ribosome tunnel. First, we found that mutations in EspP1‐25 that abolished its effects on protein targeting and protein folding altered the cross‐linking of short nascent chains to ribosomal components. Second, we found that a mutation in L22 that distorts the tunnel mimicked the effects of the EspP1‐25 mutations on protein biogenesis. Our results provide evidence that the conformation of a polypeptide inside the ribosome tunnel can influence protein folding under physiological conditions and suggest that ribosomal mutations might increase the solubility of at least some aggregation‐prone proteins produced in E. coli.

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Citations by journals

	1 2
Journal of Physical Chemistry B	Journal of Physical Chemistry B, 2, 22.22% Journal of Physical Chemistry B 2 publications, 22.22%
Antimicrobial Agents and Chemotherapy	Antimicrobial Agents and Chemotherapy, 1, 11.11% Antimicrobial Agents and Chemotherapy 1 publication, 11.11%
Frontiers in Molecular Biosciences	Frontiers in Molecular Biosciences, 1, 11.11% Frontiers in Molecular Biosciences 1 publication, 11.11%
eLife	eLife, 1, 11.11% eLife 1 publication, 11.11%
	1 2

Citations by publishers

	1 2
American Chemical Society (ACS)	American Chemical Society (ACS), 2, 22.22% American Chemical Society (ACS) 2 publications, 22.22%
American Society for Microbiology	American Society for Microbiology, 1, 11.11% American Society for Microbiology 1 publication, 11.11%
Frontiers Media S.A.	Frontiers Media S.A., 1, 11.11% Frontiers Media S.A. 1 publication, 11.11%
eLife Sciences Publications	eLife Sciences Publications, 1, 11.11% eLife Sciences Publications 1 publication, 11.11%
	1 2

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Peterson J.H., Woolhead C.A., Bernstein H.D. The conformation of a nascent polypeptide inside the ribosome tunnel affects protein targeting and protein folding // Molecular Microbiology. 2010.

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Peterson J.H., Woolhead C.A., Bernstein H.D. The conformation of a nascent polypeptide inside the ribosome tunnel affects protein targeting and protein folding // Molecular Microbiology. 2010.

RIS |

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RIS Copy

TY - JOUR

DO - 10.1111/j.1365-2958.2010.07325.x

UR - https://doi.org/10.1111%2Fj.1365-2958.2010.07325.x

TI - The conformation of a nascent polypeptide inside the ribosome tunnel affects protein targeting and protein folding

T2 - Molecular Microbiology

AU - Peterson, J H

AU - Woolhead, C A

AU - Bernstein, H D

PY - 2010

DA - 2010/08/20 00:00:00

PB - Wiley

PMID - 20804452

SN - 0950-382X

SN - 1365-2958

ER -

BibTex

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BibTex Copy

@article{2010,

author = {J H Peterson and C A Woolhead and H D Bernstein},

title = {The conformation of a nascent polypeptide inside the ribosome tunnel affects protein targeting and protein folding},

journal = {Molecular Microbiology},

year = {2010},

publisher = {Wiley},

month = {aug},

url = {https://doi.org/10.1111%2Fj.1365-2958.2010.07325.x},

doi = {10.1111/j.1365-2958.2010.07325.x}

}

Found error?

Publisher

Wiley

Journal

Molecular Microbiology

Quartile SCImago

Quartile WOS

Impact factor

3.6

ISSN

0950382X (Print)
13652958 (Electronic)