Characterization of MbrC involved in bacitracin resistance in Streptococcus mutans

Norio Kitagawa, Susumu Shiota, Yukie Shibata, Toru Takeshita, Yoshihisa Yamashita

研究成果: ジャーナルへの寄稿レター

6 引用 (Scopus)

抄録

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 (D54N-MbrC) that substituted asparagine for aspartate at position 54, the predicted phosphorylation site. MbrC, but not the mutant D54N-MbrC, showed affinity for a DNA probe that contained the hypothetical mbrA promoter sequence. Furthermore, we introduced a point mutation (D54N-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.

元の言語英語
ページ(範囲)61-67
ページ数7
ジャーナルFEMS Microbiology Letters
318
発行部数1
DOI
出版物ステータス出版済み - 5 1 2011

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Bacitracin
Streptococcus mutans
Aspartic Acid
Phosphorylation
ATP-Binding Cassette Transporters
Asparagine
DNA Probes
Dental Caries
Microarray Analysis
Point Mutation
Genetic Promoter Regions

All Science Journal Classification (ASJC) codes

  • Microbiology
  • Molecular Biology
  • Genetics

これを引用

Characterization of MbrC involved in bacitracin resistance in Streptococcus mutans. / Kitagawa, Norio; Shiota, Susumu; Shibata, Yukie; Takeshita, Toru; Yamashita, Yoshihisa.

:: FEMS Microbiology Letters, 巻 318, 番号 1, 01.05.2011, p. 61-67.

研究成果: ジャーナルへの寄稿レター

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AU - Shiota, Susumu

AU - Shibata, Yukie

AU - Takeshita, Toru

AU - Yamashita, Yoshihisa

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N2 - 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 (D54N-MbrC) that substituted asparagine for aspartate at position 54, the predicted phosphorylation site. MbrC, but not the mutant D54N-MbrC, showed affinity for a DNA probe that contained the hypothetical mbrA promoter sequence. Furthermore, we introduced a point mutation (D54N-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.

AB - 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 (D54N-MbrC) that substituted asparagine for aspartate at position 54, the predicted phosphorylation site. MbrC, but not the mutant D54N-MbrC, showed affinity for a DNA probe that contained the hypothetical mbrA promoter sequence. Furthermore, we introduced a point mutation (D54N-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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