Satoshi Yoshizumi

Robert Wood Johnson University Hospital, New Brunswick, New Jersey, United States

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Publications (3)8.24 Total impact

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    ABSTRACT: MazF is an mRNA interferase that cleaves mRNAs at a specific RNA sequence. MazF from E. coli(MazF-ec) cleaves RNA at A⁁CA. To date, a large number of MazF homologues that cleave RNA at specific three- to seven-base sequenceshave been identified from bacteria to archaea. MazF-ec forms a dimer, in which the interface between the two subunits is known to be the RNA substrate-binding site. Here, we investigated the role of the two loops in MazF-ec, which are closely associated with the interface of the MazF-ec dimer. We examined whetherexchanging the loop regions of MazF-ec with those from other MazF homologues, such as MazF from Myxococcus xanthus (MazF-mx) and MazF from Mycobacterium tuberculosis (MazF-mt3), affects RNA cleavage specificity. We found that exchanging loop 2 of MazF-ec with loop 2 regions from either MazF-mx or MazF-mt3 created a new cleavage sequence at (A/U)(A/U)AA⁁C in addition to the original cleavage site, A⁁CA, while exchanging loop 1 did not alter cleavage specificity. Intriguingly, exchange of loop 2 with 8 or 12 consecutive Gly residues also resulted in a new RNA cleavage site at (A/U)(A/U)AA⁁C. The present study suggests a method for expanding the RNA cleavage repertoire of mRNA interferases, which is crucial for potential use in the regulation of specific gene expression and for biotechnological applications. Proteins 2012. © 2012 Wiley Periodicals, Inc.
    Proteins Structure Function and Bioinformatics 05/2013; 81(5). DOI:10.1002/prot.24246 · 2.63 Impact Factor
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    ABSTRACT: YoeB is a bacterial toxin encoded by the yefM-yoeB toxin-antitoxin system found in various bacterial genomes. Here, we show that Staphylococcus aureus contains two YoeB homologues, both of which function as ribosome-dependent mRNA interferases to inhibit translation initiation in a manner identical to that of YoeB-ec from Escherichia coli.
    Journal of bacteriology 08/2009; 191(18):5868-72. DOI:10.1128/JB.00623-09 · 2.81 Impact Factor
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    ABSTRACT: 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.
    Journal of bacteriology 03/2009; 191(10):3248-55. DOI:10.1128/JB.01815-08 · 2.81 Impact Factor

Publication Stats

63 Citations
8.24 Total Impact Points


  • 2013
    • Robert Wood Johnson University Hospital
      New Brunswick, New Jersey, United States
  • 2009
    • University of Louisville
      • Department of Computer Engineering and Computer Science
      Louisville, Kentucky, United States