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 language | English |
|---|---|
| Pages (from-to) | 37-41 |
| Number of pages | 5 |
| Journal | RNA |
| Volume | 18 |
| Issue number | 1 |
| DOIs | |
| State | Published - Jan 1 2012 |
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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 journal › Article
}
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
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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 -