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J. Biol. Chem., Vol. 281, Issue 37, 27046-27051, September 15, 2006

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Retention of Core Catalytic Functions by a Conserved Minimal Ribonuclease E Peptide That Lacks the Domain Required for Tetramer Formation^*

Jonathan M. Caruthers¹, Yanan Feng¹, David B. McKay², and Stanley N. Cohen^¶3

From the Departments of Structural Biology, Genetics, and ^¶Medicine, Stanford University School of Medicine, Stanford, California 94305

Ribonuclease E (RNase E) is a multifunctional endoribonuclease that has been evolutionarily conserved in both Gram-positive and Gram-negative bacteria. X-ray crystallography and biochemical studies have concluded that the Escherichia coli RNase E protein functions as a homotetramer formed by Zn linkage of dimers within a region extending from amino acid residues 416 through 529 of the 116-kDa protein. Using fragments of RNase E proteins from E. coli and Haemophilus influenzae, we show here that RNase E derivatives that are as short as 395 amino acid residues and that lack the Zn-link region shown previously to be essential for tetramer formation (i.e. amino acid residues 400–415) are catalytically active enzymes that retain the 5' to 3' scanning ability and cleavage site specificity characteristic of full-length RNase E and that also confer colony forming ability on rne null mutant bacteria. Further truncation leads to loss of these properties. Our results, which identify a minimal catalytically active RNase E sequence, indicate that contrary to current models, a tetrameric quaternary structure is not required for RNase E to carry out its core enzymatic functions.

Received for publication, March 16, 2006 , and in revised form, July 12, 2006.

^* This work was supported by Grants GM 71696 (to D. B. M.) and GM 54158 (to S. N. C.) from the National Institutes of Health and Grant MCB-9874528 (to D. B. M.) from the National Science Foundation. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ These authors contributed equally to the work, and the order of listing was determined randomly.

² To whom correspondence may be addressed: Stanford University School of Medicine, Dept. of Structural Biology, Stanford, CA 94305-5126. Tel.: 650-723-6589; Fax: 650-723-8464; E-mail: dave.mckay{at}stanford.edu. ³ To whom correspondence may be addressed: Stanford University School of Medicine, Dept. of Genetics, Stanford, CA 94305-5120. Tel.: 650-723-5315; Fax: 650-725-1536; E-mail: sncohen{at}stanford.edu.

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