Protein acetylation in prokaryotes increases stress resistance

Research output: Contribution to journalArticle

49 Citations (Scopus)

Abstract

Acetylation of lysine residues is conserved in all three kingdoms; however, its role in prokaryotes is unknown. Here we demonstrate that acetylation enables the reference bacterium Escherichia coli to withstand environmental stress. Specifically, the bacterium reaches higher cell densities and becomes more resistant to heat and oxidative stress when its proteins are acetylated as shown by deletion of the gene encoding acetyltransferase YfiQ and the gene encoding deacetylase CobB as well as by overproducing YfiQ and CobB. Furthermore, we show that the increase in oxidative stress resistance with acetylation is due to the induction of catalase activity through enhanced katG expression. We also found that two-component system proteins CpxA, PhoP, UvrY, and BasR are associated with cell catalase activity and may be responsible as the connection between bacterial acetylation and the stress response. This is the first demonstration of a specific environmental role of acetylation in prokaryotes.

Original languageEnglish (US)
Pages (from-to)846-851
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume410
Issue number4
DOIs
StatePublished - Jul 15 2011

Fingerprint

Acetylation
Gene encoding
Oxidative stress
Proteins
Catalase
Bacteria
Oxidative Stress
Acetyltransferases
Gene Deletion
Escherichia coli
Lysine
Demonstrations
Cell Count
Hot Temperature
Genes

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

@article{999ac14448e34b6093278f8ac8eba5bc,
title = "Protein acetylation in prokaryotes increases stress resistance",
abstract = "Acetylation of lysine residues is conserved in all three kingdoms; however, its role in prokaryotes is unknown. Here we demonstrate that acetylation enables the reference bacterium Escherichia coli to withstand environmental stress. Specifically, the bacterium reaches higher cell densities and becomes more resistant to heat and oxidative stress when its proteins are acetylated as shown by deletion of the gene encoding acetyltransferase YfiQ and the gene encoding deacetylase CobB as well as by overproducing YfiQ and CobB. Furthermore, we show that the increase in oxidative stress resistance with acetylation is due to the induction of catalase activity through enhanced katG expression. We also found that two-component system proteins CpxA, PhoP, UvrY, and BasR are associated with cell catalase activity and may be responsible as the connection between bacterial acetylation and the stress response. This is the first demonstration of a specific environmental role of acetylation in prokaryotes.",
author = "Qun Ma and Wood, {Thomas K.}",
year = "2011",
month = "7",
day = "15",
doi = "10.1016/j.bbrc.2011.06.076",
language = "English (US)",
volume = "410",
pages = "846--851",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Academic Press Inc.",
number = "4",

}

Protein acetylation in prokaryotes increases stress resistance. / Ma, Qun; Wood, Thomas K.

In: Biochemical and Biophysical Research Communications, Vol. 410, No. 4, 15.07.2011, p. 846-851.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Protein acetylation in prokaryotes increases stress resistance

AU - Ma, Qun

AU - Wood, Thomas K.

PY - 2011/7/15

Y1 - 2011/7/15

N2 - Acetylation of lysine residues is conserved in all three kingdoms; however, its role in prokaryotes is unknown. Here we demonstrate that acetylation enables the reference bacterium Escherichia coli to withstand environmental stress. Specifically, the bacterium reaches higher cell densities and becomes more resistant to heat and oxidative stress when its proteins are acetylated as shown by deletion of the gene encoding acetyltransferase YfiQ and the gene encoding deacetylase CobB as well as by overproducing YfiQ and CobB. Furthermore, we show that the increase in oxidative stress resistance with acetylation is due to the induction of catalase activity through enhanced katG expression. We also found that two-component system proteins CpxA, PhoP, UvrY, and BasR are associated with cell catalase activity and may be responsible as the connection between bacterial acetylation and the stress response. This is the first demonstration of a specific environmental role of acetylation in prokaryotes.

AB - Acetylation of lysine residues is conserved in all three kingdoms; however, its role in prokaryotes is unknown. Here we demonstrate that acetylation enables the reference bacterium Escherichia coli to withstand environmental stress. Specifically, the bacterium reaches higher cell densities and becomes more resistant to heat and oxidative stress when its proteins are acetylated as shown by deletion of the gene encoding acetyltransferase YfiQ and the gene encoding deacetylase CobB as well as by overproducing YfiQ and CobB. Furthermore, we show that the increase in oxidative stress resistance with acetylation is due to the induction of catalase activity through enhanced katG expression. We also found that two-component system proteins CpxA, PhoP, UvrY, and BasR are associated with cell catalase activity and may be responsible as the connection between bacterial acetylation and the stress response. This is the first demonstration of a specific environmental role of acetylation in prokaryotes.

UR - http://www.scopus.com/inward/record.url?scp=79960318555&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=79960318555&partnerID=8YFLogxK

U2 - 10.1016/j.bbrc.2011.06.076

DO - 10.1016/j.bbrc.2011.06.076

M3 - Article

C2 - 21703240

AN - SCOPUS:79960318555

VL - 410

SP - 846

EP - 851

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 4

ER -