Post-translational modification of RNase R is regulated by stress-dependent reduction in the acetylating enzyme Pka (YfiQ)

Wenxing Liang, Murray P Deutscher

Research output: Contribution to journalArticle

38 Citations (Scopus)

Abstract

RNase R is a processive exoribonuclease that plays an important role in degradation of structured RNAs in Escherichia coli. RNase R is unstable in exponential phase cells; however, under certain stress conditions, RNase R levels increase dramatically due to its stabilization. Binding of tmRNA and SmpB to the C-terminal region of RNase R is required for its instability, and this binding is regulated by acetylation of a single residue, Lys544, in exponential phase cells. RNase R is not acetylated in stationary phase. We show here that only exponential phase RNase R is acetylated because the modifying enzyme, protein lysine acetyltransferase, Pka (YfiQ), is absent from late exponential and stationary phase cells. As a consequence, newly synthesized RNase R remains unmodified. Together with the turnover of preexisting acetylated RNase R, no modified RNase R remains in stationary phase. We find that RNase R in cold-shocked cells also lacks the acetyl modification due to the absence of Pka. These data indicate that RNase R stability depends on Pka, which itself is regulated under stress conditions.

Original languageEnglish
Pages (from-to)37-41
Number of pages5
JournalRNA
Volume18
Issue number1
DOIs
StatePublished - Jan 1 2012

Fingerprint

Post Translational Protein Processing
Enzymes
ribonuclease R
Exoribonucleases
RNA Stability
Acetylation
Escherichia coli

Keywords

  • Escherichia coli
  • Post-translational modification
  • Protein stability
  • Ribonuclease

ASJC Scopus subject areas

  • Molecular Biology

Cite this

Post-translational modification of RNase R is regulated by stress-dependent reduction in the acetylating enzyme Pka (YfiQ). / Liang, Wenxing; Deutscher, Murray P.

In: RNA, Vol. 18, No. 1, 01.01.2012, p. 37-41.

Research output: Contribution to journalArticle

@article{0600079d08a9403a8577c566b7a6c73a,
title = "Post-translational modification of RNase R is regulated by stress-dependent reduction in the acetylating enzyme Pka (YfiQ)",
abstract = "RNase R is a processive exoribonuclease that plays an important role in degradation of structured RNAs in Escherichia coli. RNase R is unstable in exponential phase cells; however, under certain stress conditions, RNase R levels increase dramatically due to its stabilization. Binding of tmRNA and SmpB to the C-terminal region of RNase R is required for its instability, and this binding is regulated by acetylation of a single residue, Lys544, in exponential phase cells. RNase R is not acetylated in stationary phase. We show here that only exponential phase RNase R is acetylated because the modifying enzyme, protein lysine acetyltransferase, Pka (YfiQ), is absent from late exponential and stationary phase cells. As a consequence, newly synthesized RNase R remains unmodified. Together with the turnover of preexisting acetylated RNase R, no modified RNase R remains in stationary phase. We find that RNase R in cold-shocked cells also lacks the acetyl modification due to the absence of Pka. These data indicate that RNase R stability depends on Pka, which itself is regulated under stress conditions.",
keywords = "Escherichia coli, Post-translational modification, Protein stability, Ribonuclease",
author = "Wenxing Liang and Deutscher, {Murray P}",
year = "2012",
month = "1",
day = "1",
doi = "10.1261/rna.030213.111",
language = "English",
volume = "18",
pages = "37--41",
journal = "RNA",
issn = "1355-8382",
publisher = "Cold Spring Harbor Laboratory Press",
number = "1",

}

TY - JOUR

T1 - Post-translational modification of RNase R is regulated by stress-dependent reduction in the acetylating enzyme Pka (YfiQ)

AU - Liang, Wenxing

AU - Deutscher, Murray P

PY - 2012/1/1

Y1 - 2012/1/1

N2 - RNase R is a processive exoribonuclease that plays an important role in degradation of structured RNAs in Escherichia coli. RNase R is unstable in exponential phase cells; however, under certain stress conditions, RNase R levels increase dramatically due to its stabilization. Binding of tmRNA and SmpB to the C-terminal region of RNase R is required for its instability, and this binding is regulated by acetylation of a single residue, Lys544, in exponential phase cells. RNase R is not acetylated in stationary phase. We show here that only exponential phase RNase R is acetylated because the modifying enzyme, protein lysine acetyltransferase, Pka (YfiQ), is absent from late exponential and stationary phase cells. As a consequence, newly synthesized RNase R remains unmodified. Together with the turnover of preexisting acetylated RNase R, no modified RNase R remains in stationary phase. We find that RNase R in cold-shocked cells also lacks the acetyl modification due to the absence of Pka. These data indicate that RNase R stability depends on Pka, which itself is regulated under stress conditions.

AB - RNase R is a processive exoribonuclease that plays an important role in degradation of structured RNAs in Escherichia coli. RNase R is unstable in exponential phase cells; however, under certain stress conditions, RNase R levels increase dramatically due to its stabilization. Binding of tmRNA and SmpB to the C-terminal region of RNase R is required for its instability, and this binding is regulated by acetylation of a single residue, Lys544, in exponential phase cells. RNase R is not acetylated in stationary phase. We show here that only exponential phase RNase R is acetylated because the modifying enzyme, protein lysine acetyltransferase, Pka (YfiQ), is absent from late exponential and stationary phase cells. As a consequence, newly synthesized RNase R remains unmodified. Together with the turnover of preexisting acetylated RNase R, no modified RNase R remains in stationary phase. We find that RNase R in cold-shocked cells also lacks the acetyl modification due to the absence of Pka. These data indicate that RNase R stability depends on Pka, which itself is regulated under stress conditions.

KW - Escherichia coli

KW - Post-translational modification

KW - Protein stability

KW - Ribonuclease

UR - http://www.scopus.com/inward/record.url?scp=84055212205&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84055212205&partnerID=8YFLogxK

U2 - 10.1261/rna.030213.111

DO - 10.1261/rna.030213.111

M3 - Article

C2 - 22124017

AN - SCOPUS:84055212205

VL - 18

SP - 37

EP - 41

JO - RNA

JF - RNA

SN - 1355-8382

IS - 1

ER -