Subunit structure of Escherichia coli exonuclease VII.

L. D. Vales, B. A. Rabin, J. W. Chase

Research output: Contribution to journalArticlepeer-review

16 Scopus citations


Exonuclease VII has been purified 7,500-fold to 87% homogeneity from Escherichia coli K12 using a new purification procedure. The enzyme has been shown to be composed of two nonidentical subunits of 10,500 and 54,000 daltons. This has been confirmed by restoration of exonuclease VII activity after renaturation of denatured and purified subunits. The structure of the native enzyme consists of one large subunit and four small subunits. We have previously isolated exonuclease VII mutant strains containing defects which map at two distinct loci. Subunit-mixing experiments utilizing wild type enzyme and temperature-sensitive enzyme produced by an xseB mutant strain have shown that the xseB gene codes for the small subunit of the enzymes.

Original languageEnglish (US)
Pages (from-to)8799-8805
Number of pages7
JournalJournal of Biological Chemistry
Issue number15
StatePublished - Aug 10 1982
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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