Study on the specificity alteration of mammalian UV endonuclease III

Jae Yung Lee, Joon Kim

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

A mammalian DNA repair enzyme, UV endonuclease III which also functions as a ribosomal protein S3 (rpS3), was purified from mouse cells and characterized. UV endonuclease III was previously cloned and known to yield a peptide of 32 kDa upon expression in E. coli [Kim et al., (1995) J. Biol. Chem. 270, 13620-13629]. However, biochemically purified UV endonuclease III, which has a sedimentation coefficient of 3.2S, appears to have an additional peptide of 28 kDa. It appears that two bands were derived from one complex, judging from the comparison of the nuclease activity on the native and SDS-gel electrophoreses. UV endonuclease III becomes non-specific upon purification and this phenomenon is more significant in the case of pure fractions of the enzyme. Non-specific activity was not influenced by pH or any salt conditions.

Original languageEnglish
Pages (from-to)66-72
Number of pages7
JournalJournal of Biochemistry and Molecular Biology
Volume30
Issue number1
Publication statusPublished - 1997 Jan 31

Keywords

  • DNA repair
  • Endonuclease
  • Ribosomal protein S3
  • Specificity
  • UV damage

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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