Journal
BIOCHEMISTRY
Volume 53, Issue 4, Pages 682-689Publisher
AMER CHEMICAL SOC
DOI: 10.1021/bi401193w
Keywords
-
Categories
Funding
- Wellcome Trust [085176/Z/08/Z]
- Darwin Trust of Edinburgh
- Wellcome Trust [085176/Z/08/Z] Funding Source: Wellcome Trust
- BBSRC [BB/J000884/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/J000884/1] Funding Source: researchfish
Ask authors/readers for more resources
Most DNA transposons move from one genomic location to another by a cut-and-paste mechanism and are useful tools for genomic manipulations. Short inverted repeat (IR) DNA sequences marking each end of the transposon are recognized by a DNA transposase (encoded by the transposon itself). This enzyme cleaves the transposon ends and integrates them at a new genomic location. We report here a comparison of the biophysical and biochemical properties of two closely related and active mariner/Tc1 family DNA transposases: Mboumar-9 and Mos1. We compared the in vitro cleavage activities of the enzymes on their own IR sequences, as well as cross-recognition of their inverted repeat sequences. We found that, like Mos1, untagged recombinant Mboumar-9 transposase is a dimer and forms a stable complex with inverted repeat DNA in the presence of Mg2+ ions. Mboumar-9 transposase cleaves its inverted repeat DNA in the manner observed for Mos1 transposase. There was minimal cross,recognition of IR sequences between Mos1 and Mboumar-9 transposases, despite these enzymes having 68% identical amino acid sequences. Transposases sharing common biophysical and biochemical properties, but retaining recognition specificity toward their own IR, are a promising platform for the design of chimeric transposases with predicted and improved sequence recognition.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available