Quantifying the benefits of translation regulation in the unfolded protein response

Research output: Contribution to journalJournal articleResearchpeer-review

Standard

Quantifying the benefits of translation regulation in the unfolded protein response. / Axelsen, Jacob Bock; Sneppen, Kim.

In: Physical Biology, Vol. 1, No. 3, 01.10.2004, p. 159-165.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Axelsen, JB & Sneppen, K 2004, 'Quantifying the benefits of translation regulation in the unfolded protein response', Physical Biology, vol. 1, no. 3, pp. 159-165. https://doi.org/10.1088/1478-3967/1/3/003

APA

Axelsen, J. B., & Sneppen, K. (2004). Quantifying the benefits of translation regulation in the unfolded protein response. Physical Biology, 1(3), 159-165. https://doi.org/10.1088/1478-3967/1/3/003

Vancouver

Axelsen JB, Sneppen K. Quantifying the benefits of translation regulation in the unfolded protein response. Physical Biology. 2004 Oct 1;1(3):159-165. https://doi.org/10.1088/1478-3967/1/3/003

Author

Axelsen, Jacob Bock ; Sneppen, Kim. / Quantifying the benefits of translation regulation in the unfolded protein response. In: Physical Biology. 2004 ; Vol. 1, No. 3. pp. 159-165.

Bibtex

@article{08316b4aaa274c48ab24b060cd2f33cd,
title = "Quantifying the benefits of translation regulation in the unfolded protein response",
abstract = "Protein production can be regulated at the translation stage through modulation of mRNA activity and degradation. In the unfolded protein response in S. cerevisiae it works by regulating the conversion rate from a reservoir of passive mRNA to an active short-lived mRNA that is open for translation. We develop a mathematical model for translation regulation, and elucidate its properties in perspective of the size and timing of the unfolded protein response. Optimal response is obtained when active mRNA has high decay rate compared to both the conversion rate and the decay rate of passive mRNA. In that case the translation regulation can provide the observed pulse of chaperones that fast restore protein folding conditions in the endoplasmic reticulum. Finally, we discuss translation control in relation to other known mechanisms for stress responses. Feedback on the translation level is found to be superior to transcription when conditions necessitate a fast shift in protein concentration while retaining a small cost in terms of protein degradation.",
author = "Axelsen, {Jacob Bock} and Kim Sneppen",
year = "2004",
month = oct,
day = "1",
doi = "10.1088/1478-3967/1/3/003",
language = "English",
volume = "1",
pages = "159--165",
journal = "Physical Biology",
issn = "1478-3967",
publisher = "Institute of Physics Publishing Ltd",
number = "3",

}

RIS

TY - JOUR

T1 - Quantifying the benefits of translation regulation in the unfolded protein response

AU - Axelsen, Jacob Bock

AU - Sneppen, Kim

PY - 2004/10/1

Y1 - 2004/10/1

N2 - Protein production can be regulated at the translation stage through modulation of mRNA activity and degradation. In the unfolded protein response in S. cerevisiae it works by regulating the conversion rate from a reservoir of passive mRNA to an active short-lived mRNA that is open for translation. We develop a mathematical model for translation regulation, and elucidate its properties in perspective of the size and timing of the unfolded protein response. Optimal response is obtained when active mRNA has high decay rate compared to both the conversion rate and the decay rate of passive mRNA. In that case the translation regulation can provide the observed pulse of chaperones that fast restore protein folding conditions in the endoplasmic reticulum. Finally, we discuss translation control in relation to other known mechanisms for stress responses. Feedback on the translation level is found to be superior to transcription when conditions necessitate a fast shift in protein concentration while retaining a small cost in terms of protein degradation.

AB - Protein production can be regulated at the translation stage through modulation of mRNA activity and degradation. In the unfolded protein response in S. cerevisiae it works by regulating the conversion rate from a reservoir of passive mRNA to an active short-lived mRNA that is open for translation. We develop a mathematical model for translation regulation, and elucidate its properties in perspective of the size and timing of the unfolded protein response. Optimal response is obtained when active mRNA has high decay rate compared to both the conversion rate and the decay rate of passive mRNA. In that case the translation regulation can provide the observed pulse of chaperones that fast restore protein folding conditions in the endoplasmic reticulum. Finally, we discuss translation control in relation to other known mechanisms for stress responses. Feedback on the translation level is found to be superior to transcription when conditions necessitate a fast shift in protein concentration while retaining a small cost in terms of protein degradation.

UR - http://www.scopus.com/inward/record.url?scp=33748573290&partnerID=8YFLogxK

U2 - 10.1088/1478-3967/1/3/003

DO - 10.1088/1478-3967/1/3/003

M3 - Journal article

C2 - 16204835

AN - SCOPUS:33748573290

VL - 1

SP - 159

EP - 165

JO - Physical Biology

JF - Physical Biology

SN - 1478-3967

IS - 3

ER -

ID: 217103838