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Journal of Bacteriology, May 2009, p. 3248-3255, Vol. 191, No. 10
0021-9193/09/$08.00+0 doi:10.1128/JB.01815-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Koichi Inoue,1,
Satoshi Yoshizumi,1
Hiroshi Kobayashi,1
Yonglong Zhang,1
Ming Ouyang,2
Fuminori Kato,3
Motoyuki Sugai,3 and
Masayori Inouye1*
Department of Biochemistry, Robert Wood Johnson Medical School, Piscataway, New Jersey 08854,1 Computer Engineering and Computer Science Department, University of Louisville, Louisville, Kentucky 40292,2 Laboratory of Bacteriology, Graduate School of Biomedical Sciences, Hiroshima University, Higashi-Hiroshima City, Japan3
Received 23 December 2008/ Accepted 14 February 2009
Escherichia coli mRNA interferases, such as MazF and ChpBK, are sequence-specific endoribonucleases encoded by toxin-antitoxin (TA) systems present in its genome. A MazF homologue in Staphylococcus aureus (MazFSa) has been shown to inhibit cell growth when induced in E. coli. Here, we determined the cleavage site for MazFSa with the use of phage MS2 RNA as a substrate and CspA, an RNA chaperone, which prevents the formation of secondary structures in the RNA substrate. MazFSa specifically cleaves the RNA at a pentad sequence, U
ACAU. Bioinformatics analysis revealed that this pentad sequence is significantly abundant in several genes, including the sraP gene in the S. aureus N315 strain. This gene encodes a serine-rich protein, which is known to play an important role in adhesion of the pathogen to human tissues and thus in endovascular infection. We demonstrated that the sraP mRNA became extremely unstable in comparison with the ompA mRNA only when MazFSa was induced in E. coli. Further bioinformatics analysis indicated that the pentad sequence is also significantly abundant in the mRNAs for all the pathogenic factors in S. aureus. This observation suggests a possible regulatory relationship between the MazEFSa TA module and the pathogenicity in S. aureus.
Published ahead of print on 27 February 2009.
Both authors contributed equally to this work.
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