Published online 14 April 2005
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Ribonucleases J1 and J2: two novel endoribonucleases in B.subtilis with functional homology to E.coli RNase E
CNRS UPR9073, IBPC 13 rue P. et M. Curie, 75005 Paris, France 1CNRS UMR7637, ESPCI 10 rue Vauquelin 75005 Paris, France
*To whom correspondence should be addressed. Tel: +33 1 58 41 51 27; Fax: +33 1 58 41 50 20; Email: putzer{at}ibpc.fr
Received February 25, 2005. Revised March 24, 2005. Accepted March 24, 2005.
Many prokaryotic organisms lack an equivalent of RNase E, which plays a key role in mRNA degradation in Escherichia coli. In this paper, we report the purification and identification by mass spectrometry in Bacillus subtilis of two paralogous endoribonucleases, here named RNases J1 and J2, which share functional homologies with RNase E but no sequence similarity. Both enzymes are able to cleave the B.subtilis thrS leader at a site that can also be cleaved by E.coli RNase E. We have previously shown that cleavage at this site increases the stability of the downstream messenger. Moreover, RNases J1/J2 are sensitive to the 5' phosphorylation state of the substrate in a site-specific manner. Orthologues of RNases J1/J2, which belong to the metallo-ß-lactamase family, are evolutionarily conserved in many prokaryotic organisms, representing a new family of endoribonucleases. RNases J1/J2 appear to be implicated in regulatory processing/maturation of specific mRNAs, such as the T-box family members thrS and thrZ, but may also contribute to global mRNA degradation.
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