Journal of Photoscience

Korean Society of Photoscience (한국광과학회)
권호 표지

EXAMINATION OF TYR-264 FOR ATPase ACTIVE SITE IN E.coli RecA PROTEIN BY SITE-DIRECTED MUTAGENESIS

  • Kwon, Yong-Kook (Department and Institute of Genetic Engineering, Kyung Hee University) ;
  • Bae, Jun-Seong (Department and Institute of Genetic Engineering, Kyung Hee University) ;
  • Hahn, Tae-Ryong (Department and Institute of Genetic Engineering, Kyung Hee University)
  • Published : 1995.03.01
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Abstract

Site directed mutagenesis has been introduced to determine active site(s) and molecular structure of E. coli RecA protein. Recombinant DNAs were constructed by point mutation of Tyr-264 to Phe which assumed active site for binding and hydrolysis of ATP. RecA proteins were purified from recombinants containing wild type and mutant genes and analyzed for ATPase activity assay. Result suggests that Tyr-264 is involved in ATP binding rather than ATP hydrolysis.

Keywords

References

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