Characterization of MbrC involved in bacitracin resistance in Streptococcus mutans
Author(s) -
Kitagawa Norio,
Shiota Susumu,
Shibata Yukie,
Takeshita Toru,
Yamashita Yoshihisa
Publication year - 2011
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2011.02238.x
Subject(s) - bacitracin , mutant , streptococcus mutans , biology , point mutation , phosphorylation , asparagine , microbiology and biotechnology , biochemistry , gene , genetics , bacteria , amino acid , antibiotics
Streptococcus mutans , a major etiological agent of dental caries, is resistant to bacitracin. Microarray analysis revealed that mbrA and mbrB , encoding a putative ATP‐binding cassette transporter, are prominently induced in the presence of bacitracin. On the basis of the latest report that MbrC, a putative response regulator in a two‐component signaling system, binds the promoter region of mbrA and thus regulates its transcription, we cut into the mechanism by generating a mutant MbrC (D 54 N‐MbrC) that substituted asparagine for aspartate at position 54, the predicted phosphorylation site. MbrC, but not the mutant D 54 N‐MbrC, showed affinity for a DNA probe that contained the hypothetical mbrA promoter sequence. Furthermore, we introduced a point mutation (D 54 N‐MbrC) into UA159; this mutant strain exhibited neither mbrA induction nor resistance in the presence of bacitracin. These data suggest that the aspartate residue at position 54 of MbrC is a promising candidate for phosphorylation in a bacitracin‐sensing system and indispensable for S. mutans bacitracin resistance.
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