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Journal of Bacteriology, August 2004, p. 5376-5383, Vol. 186, No. 16
0021-9193/04/$08.00+0 DOI: 10.1128/JB.186.16.5376-5383.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.
Departments of Pharmacology and Biological Chemistry,1 Physiology and Biophysics, Mount Sinai School of Medicine of New York University, New York, New York 100292
Received 11 February 2004/ Accepted 19 May 2004
In a continuing effort to identify ribonucleases that may be involved in mRNA decay in Bacillus subtilis, fractionation of a protein extract from a triple-mutant strain that was missing three previously characterized 3'-to-5' exoribonucleases (polynucleotide phosphorylase [PNPase], RNase R, and YhaM) was undertaken. These experiments revealed the presence of a high-molecular-weight nuclease encoded by the yhcR gene that was active in the presence of Ca2+ and Mn2+. YhcR is a sugar-nonspecific nuclease that cleaves endonucleolytically to yield nucleotide 3'-monophosphate products, similar to the well-characterized micrococcal nuclease of Staphylococcus aureus. YhcR appears to be located principally in the cell wall and is likely to be a substrate for a B. subtilis sortase. Zymogram analysis suggests that YhcR is the major Ca2+-activated nuclease of B. subtilis. In addition to having a unique overall domain structure, YhcR contains a hitherto unknown structural domain that we have named "NYD," for "new YhcR domain."
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