TN7 TRANSPOSITION - TARGET DNA RECOGNITION IS MEDIATED BY MULTIPLE TN7-ENCODED PROTEINS IN A PURIFIED INVITRO SYSTEM

被引：146

作者：

BAINTON, RJ ^{[1
]}

KUBO, KM ^{[1
]}

FENG, JN ^{[1
]}

CRAIG, NL ^{[1
]}

机构：

[1] JOHNS HOPKINS UNIV, SCH MED, HOWARD HUGHES MED INST, DEPT MOLEC BIOL & GENET, BALTIMORE, MD 21205 USA

来源：

CELL | 1993年 / 72卷 / 06期

关键词：

D O I：

10.1016/0092-8674(93)90581-A

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

We have reconstituted the transposition of the bacterial transposon Tn7 into its specific insertion site attTn7 with four purified Tn7-encoded proteins, TnsA+TnsB+ TnsC+TnsD, and ATP. TnsA+TnsB+TnsC form a ''core'' recombination machine that recognizes the transposon ends and executes DNA breakage and joining; TnsD specifically recognizes attTn7. TnsA+TnsB+TnsC are specifically targeted to attTn7 through the TnsD-dependent interaction of TnsC, a nonspecific DNA-binding protein, with attTn7. Recombination appears to be activated by the assembly of a nucleoprotein complex containing the DNA substrates and Tns proteins. We suggest that TnsC plays a central role in communication between the transposon and the target DNA, particularly in directing insertion away from DNAs already containing a copy of Tn7.

引用

页码：931 / 943

页数：13

共 45 条

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[42] PURIFICATION AND CHARACTERIZATION OF THE TNSB PROTEIN OF TN7 - A TRANSPOSITION PROTEIN THAT BINDS TO THE ENDS OF TN7 [J].