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The bacteriophage Mu transposase protein can form high‐affinity protein‐DNA complexes with the ends of transposable elements of the Tn 3 family
Author(s) -
Cameron Robin K.,
Jarjour Allan M.,
Tolias Peter P.,
DuBow Michael S.
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)81141-4
Subject(s) - transposase , transposable element , bacteriophage mu , insertion sequence , transposition (logic) , biology , dna , bacteriophage , genetics , tn3 transposon , genome , p element , microbiology and biotechnology , gene , escherichia coli , linguistics , philosophy
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 IS 101 . No significant protein‐DNA complex formation was observed with DNA fragments containing the right end of the element IS 102 , 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.