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A more recent version of this article appeared on September 15, 2006 Originally published In Press as doi:10.1074/jbc.M602467200 on July 31, 2006
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Papers In Press, published online ahead of print July 19, 2006
J. Biol. Chem, 10.1074/jbc.M602467200
Submitted on March 16, 2006
Revised on July 12, 2006
Accepted on July 18, 2006

Retention of core catalytic functions by a conserved minimal RNase E peptide that lacks the domain required for tetramer formation

Jonathan M. Caruthers, Yanan Feng, David B. McKay, and Stanley N. Cohen

Genetics, Stanford University, Stanford, CA 94305-5120

Corresponding Author: sncohen{at}stanford.edu

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 (1, 2). Using fragments of RNase E proteins from E. coli and Haemophilus influenzae (H. influenzae), we show here that RNase E derivatives that are as short as 395 amino acid residues and which 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 which 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.


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