Heat Shock Triggers Assembly of tRNA Synthetases into an Active Supercomplex

Joshua Riback; Pawel Laskowski; Jamie L Scott; Edward WJ Wallace; Alexandra E Rojek; Michael H Schwartz; Tobin R Sosnick; D Allan Drummond

doi:10.1016/j.bpj.2014.11.1219

Heat Shock Triggers Assembly of tRNA Synthetases into an Active Supercomplex

Joshua Riback, Pawel Laskowski, Jamie L Scott, Edward WJ Wallace, Alexandra E Rojek, Michael H Schwartz, Tobin R Sosnick, D Allan Drummond

School of Informatics

Research output: Contribution to journal › Meeting abstract › peer-review

Abstract

Heat shock stimulates cellular production of protein folding chaperones. This response is a reaction to, and likely triggered by, protein misfolding and aggregation. Using a proteome-scale mass spectrometry screen for protein aggregation upon heat shock in vivo, we found that many components of the translational apparatus associate into high-molecular weight species. One such component is the ternary yeast multi-tRNA synthetase complex (glutamyl- and methionyl-tRNA synthetases Gus1 and Mes1 with their aminoacylation cofactor Arc1).

Original language	English
Pages (from-to)	221a
Number of pages	1
Journal	Biophysical Journal
Volume	108
Issue number	Issue 2, Supplement 1
DOIs	https://doi.org/10.1016/j.bpj.2014.11.1219
Publication status	Published - 2015

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10.1016/j.bpj.2014.11.1219

http://www.cell.com/biophysj/abstract/S0006-3495%2814%2902428-X

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title = "Heat Shock Triggers Assembly of tRNA Synthetases into an Active Supercomplex",

abstract = "Heat shock stimulates cellular production of protein folding chaperones. This response is a reaction to, and likely triggered by, protein misfolding and aggregation. Using a proteome-scale mass spectrometry screen for protein aggregation upon heat shock in vivo, we found that many components of the translational apparatus associate into high-molecular weight species. One such component is the ternary yeast multi-tRNA synthetase complex (glutamyl- and methionyl-tRNA synthetases Gus1 and Mes1 with their aminoacylation cofactor Arc1).",

author = "Joshua Riback and Pawel Laskowski and Scott, {Jamie L} and Wallace, {Edward WJ} and Rojek, {Alexandra E} and Schwartz, {Michael H} and Sosnick, {Tobin R} and Drummond, {D Allan}",

year = "2015",

doi = "10.1016/j.bpj.2014.11.1219",

language = "English",

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T1 - Heat Shock Triggers Assembly of tRNA Synthetases into an Active Supercomplex

AU - Riback, Joshua

AU - Laskowski, Pawel

AU - Scott, Jamie L

AU - Wallace, Edward WJ

AU - Rojek, Alexandra E

AU - Schwartz, Michael H

AU - Sosnick, Tobin R

AU - Drummond, D Allan

PY - 2015

Y1 - 2015

N2 - Heat shock stimulates cellular production of protein folding chaperones. This response is a reaction to, and likely triggered by, protein misfolding and aggregation. Using a proteome-scale mass spectrometry screen for protein aggregation upon heat shock in vivo, we found that many components of the translational apparatus associate into high-molecular weight species. One such component is the ternary yeast multi-tRNA synthetase complex (glutamyl- and methionyl-tRNA synthetases Gus1 and Mes1 with their aminoacylation cofactor Arc1).

AB - Heat shock stimulates cellular production of protein folding chaperones. This response is a reaction to, and likely triggered by, protein misfolding and aggregation. Using a proteome-scale mass spectrometry screen for protein aggregation upon heat shock in vivo, we found that many components of the translational apparatus associate into high-molecular weight species. One such component is the ternary yeast multi-tRNA synthetase complex (glutamyl- and methionyl-tRNA synthetases Gus1 and Mes1 with their aminoacylation cofactor Arc1).

U2 - 10.1016/j.bpj.2014.11.1219

DO - 10.1016/j.bpj.2014.11.1219

M3 - Meeting abstract

SN - 0006-3495

VL - 108

SP - 221a

JO - Biophysical Journal

JF - Biophysical Journal

IS - Issue 2, Supplement 1

ER -

Heat Shock Triggers Assembly of tRNA Synthetases into an Active Supercomplex

Abstract

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