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PMID: 9826663 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Host factor I, Hfq, binds to Escherichia coli ompA mRNA in a growth rate-dependent fashion and regulates its stability.

Vytvytska O, Jakobsen JS, Balcunaite G, Andersen JS, Baccarini M, von Gabain A

Abstract

The stability of the ompA mRNA depends on the bacterial growth rate. The 5' untranslated region is the stability determinant of this transcript and the target of the endoribonuclease, RNase E, the key player of mRNA degradation. An RNA-binding protein with affinity for the 5' untranslated region ompA was purified and identified as Hfq, a host factor initially recognized for its function in phage Qbeta replication. The ompA RNA-binding activity parallels the amount of Hfq, which is elevated in bacteria cultured at slow growth rate, a condition leading to facilitated degradation of the ompA mRNA. In hfq mutant cells with a deficient Hfq gene product, the RNA-binding activity is missing, and analysis of the ompA mRNA showed that the growth-rate dependence of degradation is lost. Furthermore, the half-life of the ompA mRNA is prolonged in the mutant cells, irrespective of growth rate. Hfq has no affinity for the lpp transcript whose degradation, like that of bulk mRNA, is not affected by bacterial growth rate. Compatible with our results, we found that the intracellular concentration of RNase E and its associated degradosome components is independent of bacterial growth rate. Thus our results suggest a regulatory role for Hfq that specifically facilitates the ompA mRNA degradation in a growth rate-dependent manner.

MeSH Terms
Bacterial Outer Membrane Proteins/genetics Carrier Proteins/biosynthesis,isolation & purification,metabolism Escherichia coli/genetics,growth & development,metabolism Escherichia coli Proteins Host Factor 1 Protein Integration Host Factors Kinetics RNA, Bacterial/genetics,metabolism RNA, Messenger/genetics,metabolism RNA-Binding Proteins/biosynthesis,metabolism Transcription, Genetic
Chemicals
Bacterial Outer Membrane Proteins Carrier Proteins Escherichia coli Proteins Host Factor 1 Protein Integration Host Factors RNA, Bacterial RNA, Messenger RNA-Binding Proteins integration host factor, E coli OMPA outer membrane proteins
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Vytvytska O
Institute of Microbiology and Genetics, Vienna Biocenter, University of Vienna, Dr. Bohr-Gasse 9, A-1030 Vienna, Austria.
Jakobsen J S
Balcunaite G
Andersen J S
Baccarini M
von Gabain A
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1998-11-24
Pages
14118-23
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC24336
Subset
IM
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