Difference between revisions of "Part:BBa K1413043:Design"
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===Source===
 
===Source===
  
−
This part was given by a member of the institute of systems and synthetic biology (Evry, France)
+
This part was given by a member of the institute of systems and synthetic biology (Evry, France, the researcher Brian Jester.
  
 
===References===
 
===References===
 
Bender, J., & Kleckner, N. (1988). Genetic Evidence That TnlO Transposes by a Nonreplicative Mechanism, 45, 801–815.
 
Bender, J., & Kleckner, N. (1988). Genetic Evidence That TnlO Transposes by a Nonreplicative Mechanism, 45, 801–815.
 +
 
Biology, C. (1996). Two Classes of TnlO Transposase Mutants That Suppress Mutations i n, (1972).  
 
Biology, C. (1996). Two Classes of TnlO Transposase Mutants That Suppress Mutations i n, (1972).  
−
Chalmers, R. M. (1995). Identification characterization pre-cleavage complex early transposition, 14(17), 4374–4383.  
+
 
 +
Chalmers, R. M. (1995). Identification characterization pre-cleavage complex early transposition, 14(17), 4374–4383.
 +
 
Crellin, P., & Chalmers, R. (2001). Protein±DNA contacts and conformational changes in the Tn 10 transpososome during assembly and activation for cleavage, 20(14).  
 
Crellin, P., & Chalmers, R. (2001). Protein±DNA contacts and conformational changes in the Tn 10 transpososome during assembly and activation for cleavage, 20(14).  
 +
 
Foster, T. J., Davis, M. A., Roberts, D. E., Takeshita, K., Kleckner, N., & Laboratories, T. B. (1981). Genetic Organization of Transposon TnlO,23(January), 201–213.  
 
Foster, T. J., Davis, M. A., Roberts, D. E., Takeshita, K., Kleckner, N., & Laboratories, T. B. (1981). Genetic Organization of Transposon TnlO,23(January), 201–213.  
 +
 
Humayun, S., Wardle, S. J., Shilton, B. H., Pribil, P. a, Liburd, J., & Haniford, D. B. (2005). Tn10 transposase mutants with altered transpososome unfolding properties are defective in hairpin formation. Journal of Molecular Biology, 346(3), 703–16. doi:10.1016/j.jmb.2004.12.009
 
Humayun, S., Wardle, S. J., Shilton, B. H., Pribil, P. a, Liburd, J., & Haniford, D. B. (2005). Tn10 transposase mutants with altered transpososome unfolding properties are defective in hairpin formation. Journal of Molecular Biology, 346(3), 703–16. doi:10.1016/j.jmb.2004.12.009

Latest revision as of 04:24, 2 November 2014

Transposase Tn10


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    INCOMPATIBLE WITH RFC[12]
    Illegal NheI site found at 244
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]


Design Notes

This part follows rules of RFC92, compatible with RFC10. The complex Tn10/IS10 is involved in the non-replicative cut-and-paste mechanism. The transposable segment is excised at its ends and is then re-inserted randomly in a DNA site.

The Tn10 transposase protein is made of 402 amino-acids, which recognises inverted repeats insertion sequence; Is10-right and Is10-left. The Tn10 protein expression is strongly regulated by various positive and negative regulation mechanisms.


Source

This part was given by a member of the institute of systems and synthetic biology (Evry, France, the researcher Brian Jester.

References

Bender, J., & Kleckner, N. (1988). Genetic Evidence That TnlO Transposes by a Nonreplicative Mechanism, 45, 801–815.

Biology, C. (1996). Two Classes of TnlO Transposase Mutants That Suppress Mutations i n, (1972).

Chalmers, R. M. (1995). Identification characterization pre-cleavage complex early transposition, 14(17), 4374–4383.

Crellin, P., & Chalmers, R. (2001). Protein±DNA contacts and conformational changes in the Tn 10 transpososome during assembly and activation for cleavage, 20(14).

Foster, T. J., Davis, M. A., Roberts, D. E., Takeshita, K., Kleckner, N., & Laboratories, T. B. (1981). Genetic Organization of Transposon TnlO,23(January), 201–213.

Humayun, S., Wardle, S. J., Shilton, B. H., Pribil, P. a, Liburd, J., & Haniford, D. B. (2005). Tn10 transposase mutants with altered transpososome unfolding properties are defective in hairpin formation. Journal of Molecular Biology, 346(3), 703–16. doi:10.1016/j.jmb.2004.12.009