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J Bacteriol, May 1998, p. 2779-2781, Vol. 180, No. 10
Department of Biochemistry and Molecular
Biology, University of Miami School of Medicine, Miami, Florida
33101-6129
Received 18 December 1997/Accepted 6 March 1998
Oligoribonuclease, a 3'-to-5' exoribonuclease specific for small
oligoribonucleotides, was purified to homogeneity from extracts of
Escherichia coli. The purified protein is an
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Copyright © 1998, American Society for Microbiology. All rights reserved.
Oligoribonuclease Is Encoded by a Highly Conserved
Gene in the 3'-5' Exonuclease Superfamily

and
2 dimer of
40 kDa. NH2-terminal sequence analysis of the protein
identified the gene encoding oligoribonuclease as yjeR
(o204a), a previously reported open reading frame located
at 94 min on the E. coli chromosome. However, as a
consequence of the sequence information, the translation start site of
this open reading frame has been revised. Cloning of yjeR
led to overexpression of oligoribonuclease activity, and interruption
of the cloned gene with a kanamycin resistance cassette eliminated the
overexpression. On the basis of these data, we propose that
yjeR be renamed orn. Orthologs of
oligoribonuclease are present in a wide range of organisms, extending
up to humans.
*
Corresponding author. Mailing address: Department of
Biochemistry and Molecular Biology, University of Miami School of
Medicine, P.O. Box 016129, Miami, FL 33101-6129. Phone: (305) 243-3150. Fax: (305) 243-3955. E-mail:
mdeutsch{at}mednet.med.miami.edu.
Present address: Department of Neuroscience, Tufts University
Medical School, Boston, MA.
Present address: Institute of Biophysics, Academia Sinica,
Beijing, China.
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