The bacteriophage Mu transposase protein can form high‐affinity protein‐DNA complexes with the ends of transposable elements of the Tn 3 family

FEBS Letters

Tolias, Peter P.¹  Jarjour, Allan M.¹  DuBow, Michael S.¹  Cameron, Robin K.¹ 

[1] McGill University, Department of Microbiology and Immunology, 3775 University Street, Montreal, Quebec H3A 2B4, Canada

关键词: Transposase protein;    Class II prokaryotic transposon;    Protein-DNA recognition;    Phage Mu;    bp;    base pair;    CT;    calf thymus;    Tn;    transposable element;    IS;    insertion sequence;    Pu;    purine;    kb;    kilobase pair;   

DOI  :  10.1016/0014-5793(88)81141-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The 37 kb transposable bacteriophage Mu genome encodes a transposase protein which can recognize and bind to a consensus sequence repeated three times at each extremity of its genome. A subset of this consensus sequence (5′-PuCGAAA(A)-3′) is found in the ends of many class II prokaryotic transposable elements. These elements, like phage Mu, cause 5 bp duplications at the site of element insertion, and transpose by a cointegrate mechanism. Using the band retardation assay, we have found that crude protein extracts containing overexpressed Mu transposase can form high-affinity protein-DNA complexes with Mu att R and the ends of the class II elements Tn 3 (right) and IS101. No significant protein-DNA complex formation was observed with DNA fragments containing the right end of the element IS102, or a non-specific pBR322 fragment of similar size. These results suggest that the Mu transposase protein can specifically recognize the ends of other class II transposable elements and that these elements may be evolutionarily related.

【 授权许可】

Unknown