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Nucleic Acids Research Advance Access originally published online on August 8, 2008
Nucleic Acids Research 2008 36(16):5306-5318; doi:10.1093/nar/gkn476
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Nucleic Acids Research, 2008, Vol. 36, No. 16 5306-5318
© 2008 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Molecular Biology

Intragenic suppressors of temperature-sensitive rne mutations lead to the dissociation of RNase E activity on mRNA and tRNA substrates in Escherichia coli

Tariq Perwez1, Danyal Hami1, Valerie F. Maples1, Zhao Min2, Bi-Cheng Wang2 and Sidney R. Kushner1,*

1Department of Genetics and 2Department of Biochemistry and Molecular Biology, University of Georgia, Athens, GA 30602, USA

*To whom correspondence should be addressed. Tel: 706 542 8000; Fax: 706 542 3910; Email: skushner{at}uga.edu

Received April 14, 2008. Revised July 2, 2008. Accepted July 8, 2008.

RNase E of Escherichia coli is an essential endoribonuclease that is involved in many aspects of RNA metabolism. Point mutations in the S1 RNA-binding domain of RNase E (rne-1 and rne-3071) lead to temperature-sensitive growth along with defects in 5S rRNA processing, mRNA decay and tRNA maturation. However, it is not clear whether RNase E acts similarly on all kinds of RNA substrates. Here we report the isolation and characterization of three independent intragenic second-site suppressors of the rne-1 and rne-3071 alleles that demonstrate for the first time the dissociation of the in vivo activity of RNase E on mRNA versus tRNA and rRNA substrates. Specifically, tRNA maturation and 9S rRNA processing were restored to wild-type levels in each of the three suppressor mutants (rne-1/172, rne-1/186 and rne-1/187), while mRNA decay and autoregulation of RNase E protein levels remained as defective as in the rne-1 single mutant. Each single amino acid substitution (Gly->Ala at amino acid 172; Phe -> Cys at amino acid 186 and Arg -> Leu at amino acid 187) mapped within the 5' sensor region of the RNase E protein. Molecular models of RNase E suggest how suppression may occur.

Present addresses: Danyal Hami, University Program in Genetics and Genomics, Duke University, Durham, NC 27710, USA Zhao Min, Department of Cancer Biology, Scripps Florida, Jupiter, FL 33458, USA


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