Isolation and characterization of endonuclease J: a sequence-specific endonuclease cleaving immunoglobulin genes.
Isolation and characterization of endonuclease J: a sequence-specific endonuclease cleaving immunoglobulin genes.
复制标题
核酸内切酶 J 的分离和表征：一种序列特异性核酸内切酶，可切割免疫球蛋白基因。
DOI：
10.1093/nar/12.15.5995
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发表时间：
1984
影响因子：
14.9
通讯作者：
Tasuku Honjo
中科院分区：
文献类型：
--
作者：
Tohru Kataoka;Sigeru Kondo;Miyuki Nishi;Mieko Kodaira;Tasuku Honjo
An endonuclease activity which cleaves close to the recombination sites of the immunoglobulin 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.
