Incipient complex formation between AP endonucleases and DNA containing AP site: a vital role of the tryptophan residue.
To elucidate whether the tryptophan residues in the vicinity of the catalytic site are involved in AP site recognition and are critical for AP endonuclease activity, the AP endonucleases of the four subtypes in the ExoIII AP endonuclease family were characterized and compared the positions of the tryptophan residues. The positions of the catalytic amino acid residues, corresponding to Glu-34, Asp-229, and His-259 of ExoIII, are strictly conserved. On the other hand, the positions of the tryptophan residues, which are critical to the incipient complex formation, do not exist at a fixed position. There are four patterns at the position of the essential tryptophan residue.
Yamada
Yasunori
Y
Depqrtment of Applied Biology, Faculty of Textile Science and Technology, Shinshu University, Ueda, Nagano 386-8567, Japan.
Kodera
Takuya
T
Ohishi
Kaori
K
Kaneda
Kohichi
K
Shida
Toshio
T
D000595:Amino Acid Sequence; D004247:DNA / Q000378:metabolism; D043603:DNA-(Apurinic or Apyrimidinic Site) Lyase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D005090:Exodeoxyribonucleases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D016415:Sequence Alignment; D014364:Tryptophan / Q000737:chemistry*
D014364:Tryptophan; D004247:DNA; D005090:Exodeoxyribonucleases; C020133:exodeoxyribonuclease III; D043603:DNA-(Apurinic or Apyrimidinic Site) Lyase