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The H2TH-like motif of the Escherichia coli multifunctional protein KsgA is required for DNA binding involved in DNA repair and the suppression of mutation frequencies.

Yuichiro HayashiMasafumi FunakoshiKaname HirosawaQiu-Mei Zhang-Akiyama
Published in: Genes and environment : the official journal of the Japanese Environmental Mutagen Society (2023)
The present results confirmed that one enzyme exhibited two activities and revealed that the C-terminal (214-273) amino acids of KsgA were highly similar to the H2TH structural domain, exhibited DNA-binding activity, and inhibited spontaneous mutations. This site is not essential for dimethyltransferase activity.
Keyphrases
  • dna binding
  • dna repair
  • transcription factor
  • amino acid
  • escherichia coli
  • dna damage
  • drug delivery
  • cancer therapy
  • dna damage response
  • staphylococcus aureus
  • cystic fibrosis
  • pseudomonas aeruginosa
  • biofilm formation