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Nucleic Acids Research, 1984, Vol. 12, No. 15 5995-6010
© 1984

ENZYMOLOGY

Isolation and characterization of endonuclease J: a sequence-specific endonuclease cleaving immunoglobulin genes

Tohru Kataoka1, Sigeru Kondo, Miyuki Nishi, Mieko Kodaira and Tasuku Honjo*

Department of Genetics, Osaka University Medical School 4-3-57, Nakanoshima Kita-ku, Osaka

*To whom correspondence should be addressed

Received June 4, 1984. Accepted July 10, 1984.

An endonuclease activity which cleaves close to the recombination sites of the imnunoglobulin JK segments was found in extracts of chicken bursa of Fabricius and characterized after partial purification. The enzyme preparation also cleaved a VK segment at its 3' end. A similar activity was found in mouse liver, mouse myelomas and Hela cells. The enzyme designated as endonuclease J introduces double-stranded cleavages preferentially at sequences containing G clusters of pBR322 as well as the JK segments. However, not all the G clusters were cleaved by endonuclease J, suggesting that the enzyme recognizes additional sequences. Deletion of the conserved nonamer (GGTTTTTGT) located immediately 5' to the JK4 segment drastically reduced the cleavage activity of its immediate downstream G cluster. Although biological function of endonuclease J is not clear at this stage, the possibilities of its involvement in the immunoglobulin gene recombination and general recombination were discussed.

1Present address: Cold Spring Harbor Laboratory, P.O.Box 100, Cold Spring Harbor, New York 11724, U.S.A.


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