Temperature-dependent DNA binding of DicA protein in vivo and in vitro

In vivo와 in vitro에서 DicA 단백질의 온도 의존적 DNA 결합

  • Lee, Yonho (Department of Biological Sciences, College of Biological Sciences and Biotechnology, Chungnam National University) ;
  • Yun, Sang Hoon (Alteogen) ;
  • Lim, Heon M. (Department of Biological Sciences, College of Biological Sciences and Biotechnology, Chungnam National University)
  • 이연호 (충남대학교 생명시스템과학대학 생물과학과) ;
  • 윤상훈 ((주)알테오젠) ;
  • 임헌만 (충남대학교 생명시스템과학대학 생물과학과)
  • Received : 2019.02.27
  • Accepted : 2019.06.26
  • Published : 2019.09.30


In Escherichia coli, DicA protein is involved in cell division control. DicA protein is known to bind DNA better at $25^{\circ}C$ than at $37^{\circ}C$. However, the molecular cause of the temperature dependent binding is not clear. In this study, we investigated how DicA binds DNA and why its DNA binding activity depends on temperature. An unique in vivo DNA binding assay developed in this laboratory showed that unlike the homologous proteins such as RovA or SlyA, DicA uses its N-terminal domain for DNA binding. The in vivo DNA binding assay of DicA also demonstrated that the temperature-dependent DNA binding activity does not come from Cnu or H-NS that is known to bind DNA better at $25^{\circ}C$ than at $37^{\circ}C$. Electrophoretic Mobility Shift Assay (EMSA), when performed with purified DicA protein, did not show temperature-dependent DicA binding activity. However when EMSA was performed with crude protein from WT E. coli cells, temperature-dependent DicA binding activity was observed, suggesting that there is a factor(s) that confers temperature DNA binding activity of DicA in vivo.


Escherichia coli;DicA;DNA binding;filamentous growth;temperature-dependent DNA binding activity


Supported by : 충남대학교


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