Positional information within the Mu transposase tetramer: Catalytic contributions of individual monomers

被引：34

作者：

Yang, JY ^{[1
]}

Jayaram, M ^{[1
]}

Harshey, RM ^{[1
]}

机构：

[1] UNIV TEXAS,DEPT MICROBIOL,AUSTIN,TX 78712

来源：

CELL | 1996年 / 85卷 / 03期

基金：

美国国家卫生研究院;

关键词：

D O I：

10.1016/S0092-8674(00)81122-8

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：

The strand cleavage and strand transfer reactions of Mu DNA transposition require structural/catalytic contributions from separate polypeptide domains of individual transposase (MuA) monomers within the functional MuA tetramer. Based on catalytic complementation between two inactive MuA variants, we have derived certain rules by which the physical location of a MuA monomer within the transposition complex specifies its role in DNA breakage and transfer. During strand transfer, MuA monomers contributing domain II to the reaction occupy R1 (the subsite proximal to the strand-transferred nucleotide), while those contributing domain III alpha occupy R2. The positions of the monomers contributing these two domains appear to be reversed during DNA cleavage.

引用

页码：447 / 455

页数：9

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