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M108627200v1
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Papers In Press, published online ahead of print October 4, 2001
J. Biol. Chem, 10.1074/jbc.M108627200
Submitted on September 6, 2001
Revised on October 4, 2001
Accepted on October 4, 2001

Structure and function of the E. coli RecE protein, a member of the RecB nuclease domain family

Hoshing Wan Chang and Douglas A. Julin

University of Maryland, College Park, MD 20742

Corresponding Author: dj13{at}umail.umd.edu

The RecB subunit of the E. coli RecBCD enzyme has both helicase and nuclease activities. The helicase function was localized to an amino-terminal domain while the nuclease activity was found in a carboxyl-terminal domain. Recent analysis has uncovered a group of proteins that have weak amino acid sequence similarity to the RecB nuclease domain and that are proposed to constitute a family of related proteins (Aravind, L., Walker, D. R., and Koonin, E. V. (1999) Nucleic Acids Res. 27, 1223-1242). One is the E. coli RecE protein (Exonuclease VIII), an ATP-independent exonuclease that degrades the 5'-terminated strand of double-stranded DNA. We have made mutations in several residues of RecE that align with the critical residues of RecB, and find that the mutations reduce or abolish the nuclease activity of RecE but do not affect the enzyme binding to linear double-stranded DNA. Proteolysis experiments with subtilisin show that a stable 34 kilodalton carboxyl-terminal domain that contains these critical residues has nuclease activity, while no stable proteolytic fragments accumulate from the amino-terminal portion of RecE. These results show that RecE has a nuclease domain and active site that are similar to RecB, in spite of the very weak sequence similarity between the two proteins. These similarities support the hypothesis that the nuclease domains of the two proteins are evolutionarily related.


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