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

Authors :
Manuela Baccarini
Oresta Vytvytska
Gina Balcunaite
Jimmy S. Jakobsen
Jens S. Andersen
Alexander von Gabain
Source :
Vytvytska, O, Jakobsen, J S, Balcunaite, G, Andersen, J S, Baccarini, M & von Gabain, A 1998, ' Host factor I, Hfq, binds to Escherichia coli ompA mRNA in a growth rate-dependent fashion and regulates its stability. ', Proceedings of the National Academy of Science of the United States of America, vol. 95, no. 24, pp. 14118-23 . https://doi.org/10.1073/pnas.95.24.14118
Publication Year :
1998
Publisher :
Proceedings of the National Academy of Sciences, 1998.

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 Qβ 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.

Details

ISSN :
10916490 and 00278424
Volume :
95
Database :
OpenAIRE
Journal :
Proceedings of the National Academy of Sciences
Accession number :
edsair.doi.dedup.....d1a47040c7568134eedf3541acb0316a