Structural highlights
Function
[TNSA_ECOLX] Required for Tn7 transposition. Forms the transposase, together with TnsB. TnsA executes the 5'-DNA strand breakage reaction. TnsABC and TnsD promote high-frequency insertion of Tn7 into a specific target site known as ATT-Tn7 whereas TnsABC and TnsD promote low-frequency insertion into many different sites.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Transposition requires a coordinated series of DNA breakage and joining reactions. The Tn7 transposase contains two proteins: TnsA, which carries out DNA breakage at the 5' ends of the transposon, and TnsB, which carries out breakage and joining at the 3' ends of the transposon. TnsB is a member of the retroviral integrase superfamily whose hallmark is a conserved DDE motif. We report here the structure of TnsA at 2.4 A resolution. Surprisingly, the TnsA fold is that of a type II restriction endonuclease. Thus, Tn7 transposition involves a collaboration between polypeptides, one containing a DDE motif and one that does not. This result indicates that the range of biological processes that utilize restriction enzyme-like folds also includes DNA transposition.
Unexpected structural diversity in DNA recombination: the restriction endonuclease connection.,Hickman AB, Li Y, Mathew SV, May EW, Craig NL, Dyda F Mol Cell. 2000 Jun;5(6):1025-34. PMID:10911996[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Sarnovsky RJ, May EW, Craig NL. The Tn7 transposase is a heteromeric complex in which DNA breakage and joining activities are distributed between different gene products. EMBO J. 1996 Nov 15;15(22):6348-61. PMID:8947057
- ↑ Biery MC, Lopata M, Craig NL. A minimal system for Tn7 transposition: the transposon-encoded proteins TnsA and TnsB can execute DNA breakage and joining reactions that generate circularized Tn7 species. J Mol Biol. 2000 Mar 17;297(1):25-37. PMID:10704304 doi:http://dx.doi.org/10.1006/jmbi.2000.3558
- ↑ Hickman AB, Li Y, Mathew SV, May EW, Craig NL, Dyda F. Unexpected structural diversity in DNA recombination: the restriction endonuclease connection. Mol Cell. 2000 Jun;5(6):1025-34. PMID:10911996
