Article Abstract:
The HIV integrase, avian sarcoma virus (ASV) integrase, and Mu transposase are transposition enzymes that control the cleavage and joining of the DNA of the transposable element into the host DNA. Structure studies using x-ray crystallography show that the catalytic site of Mu transposase is composed of the 248th to the 574th amino acid residues. The domain contains an N-terminal and a C-terminal. The catalytic domain of HIV integrase, composed of the 50th to the 212th amino acids, is similar to that of the ASV integrase, containing the 52nd to the 207th amino acids.
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Article Abstract:
A study was conducted to ascertain which of the six half res sites must be occupied by a 2,3'-proficient resolvase protomer for effective synapsis and recombination. This complex process is accomplished by the 2,3' interaction between resolvase dimers. To determine the half sites of res, oriented resolvase heterodimers were applied. For synapsis, 2,3' proficient interface is required at four subunits at sites II-L and III-L. For recombination, I-R and III-R also require 2,3' proficient subunits. The results are discussed.
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Article Abstract:
A study was conducted to determine the effects of architectural protein IHF and negative DNA supercoiling on Tn10/IS10 transposition. Circular miniTn10 plasmid substrates were utilized to determine the in vitro reactions of Tn10 translocation. Results revealed that the interaction of IHF and supercoiling influences Tn10 transposition in two distinct ways and IHF can modulate complex protein/DNA reactions.
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