Document Detail


Post-translational modification of RNase R is regulated by stress-dependent reduction in the acetylating enzyme Pka (YfiQ).
MedLine Citation:
PMID:  22124017     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
Wenxing Liang; Murray P Deutscher
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural     Date:  2011-11-28
Journal Detail:
Title:  RNA (New York, N.Y.)     Volume:  18     ISSN:  1469-9001     ISO Abbreviation:  RNA     Publication Date:  2012 Jan 
Date Detail:
Created Date:  2011-12-14     Completed Date:  2012-02-06     Revised Date:  2013-06-27    
Medline Journal Info:
Nlm Unique ID:  9509184     Medline TA:  RNA     Country:  United States    
Other Details:
Languages:  eng     Pagination:  37-41     Citation Subset:  IM    
Affiliation:
Department of Biochemistry and Molecular Biology, Miller School of Medicine, University of Miami, Miami, Florida 33101, USA.
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MeSH Terms
Descriptor/Qualifier:
Acetyltransferases / metabolism*
Enzyme Stability
Escherichia coli / enzymology*,  genetics,  growth & development
Escherichia coli Proteins / metabolism*
Exoribonucleases / genetics,  metabolism*
Protein Processing, Post-Translational*
RNA, Bacterial / metabolism
Stress, Physiological*
Grant Support
ID/Acronym/Agency:
GM16317/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/Escherichia coli Proteins; 0/RNA, Bacterial; 0/tmRNA; EC 2.3.1.-/Acetyltransferases; EC 2.3.1.-/acetyl-CoA synthetase acetylase, E coli; EC 3.1.-/Exoribonucleases; EC 3.1.27.-/ribonuclease R
Comments/Corrections

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