Transposase: Difference between revisions

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<StructureSection load='3ecp' size='450' side='right' caption='Structure of Tn5 transposase complex with DNA and glycerol (PDB code [[3ecp]]).' scene=''>
<StructureSection load='3ecp' size='350' side='right' caption='Structure of Tn5 transposase complex with DNA and glycerol (PDB code [[3ecp]]).' scene='59/596996/Cv/8'>
__TOC__
__TOC__
== Function ==
== Function ==


'''Transposases''' bind to the ends of a transposon and catalyze its movement to another part of the genome by a cut-and-paste mechanism<ref>PMID:19478801</ref>.    <br />
'''Transposases''' or '''transposition proteins''' bind to the ends of a transposon and catalyze its movement to another part of the genome by a cut-and-paste mechanism<ref>PMID:19478801</ref>.    <br />
*'''Mu transposase''' (MuA) is essential for integration, replication-transposition and excision of bacteriophage Mu DNA into multiple sites of bacterial genome.  Mu transposition occurs within the transposome which is a protein-DNA complex which includes 4 subunits of MuA<ref>PMID:7628012</ref>.<br />
*'''Mu transposase''' (MuA) is essential for integration, replication-transposition and excision of bacteriophage Mu DNA into multiple sites of bacterial genome.  Mu transposition occurs within the transposome which is a protein-DNA complex which includes 4 subunits of MuA<ref>PMID:7628012</ref>.<br />
*'''Hermes transposase''' is a fly protein<ref>PMID:19450689</ref>.<br />
*'''Hermes transposase''' is a fly protein<ref>PMID:19450689</ref>.<br />
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== Structural highlights ==
== Structural highlights ==
Transposase contains a <scene name='59/596996/Cv/3'>DDE motif in its active site</scene><ref>PMID:18790806</ref> enabling it to coordinate the binding of divalent metal ions.  The metal ions affect transposase reactivity. The DDE motif is conserved in transposases and retroviral integrases and is essential for their activity.
<scene name='59/596996/Cv/9'>The Biological Assembly of Tn5 transposase is homodimer</scene> (PDB code [[3ecp]]). Transposase contains a <scene name='59/596996/Cv/7'>DDE motif in its active site</scene><ref>PMID:18790806</ref> enabling it to coordinate the binding of divalent metal ions.  The metal ions affect transposase reactivity. The DDE motif is conserved in transposases and retroviral integrases and is essential for their activity.
</StructureSection>
 
==3D structures of transposase==
==3D structures of transposase==
[[Transposase 3D structures]]


Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
</StructureSection>
{{#tree:id=OrganizedByTopic|openlevels=0|
 
*Mu transposase
 
**[[1tns]], [[1tnt]] – MuMuA DNA-binding domain – enterobacteria phage Mu - NMR<br />
**[[1bcm]], [[1bco]] – MuMuA core domain <br />
**[[2ezh]], [[2ezi]] – MuMuA Iγ subdomain - NMR<br />
**[[2ezk]] – MuMuA Iβ subdomain - NMR<br />
**[[4fcy]] – MuMuA + DNA <br />
 
*Hermes transposase
 
**[[2bw3]] – fTra (mutant) - fly<br />
**[[4d1q]] – fTra (mutant) + DNA <br />
 
*Dra2 transposase
 
**[[2xm3]] – Dra2 + Dra2 transposase binding element + DNA – ''Deinococcus radiodurans'' <br />
**[[2xma]], [[2xqc]] – Dra2 + DNA <br />
**[[2xo6]] – Dra2 (mutant) + DNA <br />
 
*Tn5 transposase
 
**[[1muh]], [[1mus]], [[1mm8]], [[3ecp]], [[4dm0]] – EcTn5 (mutant) + DNA – ''Escherichia coli''<br />
 
*Tn7 transposase
 
**[[5d17]] – EcTn7 C terminal  <br />
**[[5d16]] – EcTn7 C terminal (mutant) <br />
 
*Mos1 transposase
 
**[[2f7t]] – DmMos1 catalytic domain (mutant) – ''Drosophila mauritiana''<br />
**[[4u7b]], [[5hoo]] – DmMos1 + DNA <br />
**[[3hos]], [[3hot]], [[4r79]] – DmMos1 (mutant) + DNA <br />
**[[4mda]], [[4mdb]] – DmMos1 catalytic domain (mutant) + drug<br />
 
*Tc3 transposase
 
**[[1tc3]], [[1u78]] – Tc3 DNA-binding domain (mutant) + DNA – ''Caenorhabditis elegans''<br />
 
*Orfa transposase (Is608)
 
**[[2a6m]] – HpOrfa – ''Helicobacter pylori''<br />
**[[2vhg]], [[2a6o]], [[2vic]], [[2vih]], [[2vju]], [[2vjv]]  – HpOrfa + DNA <br />
 
*Sleeping beauty transposase
 
**[[5cr4]] – SB catalytic domain – synthetic<br />
**[[5unk]] – RED domain – ''Oncorhynchus mykiss'' - NMR<br />
 
}}


== References ==
== References ==

Latest revision as of 18:29, 28 December 2020

Function

Transposases or transposition proteins bind to the ends of a transposon and catalyze its movement to another part of the genome by a cut-and-paste mechanism[1].

  • Mu transposase (MuA) is essential for integration, replication-transposition and excision of bacteriophage Mu DNA into multiple sites of bacterial genome. Mu transposition occurs within the transposome which is a protein-DNA complex which includes 4 subunits of MuA[2].
  • Hermes transposase is a fly protein[3].
  • Dra2 transposase is a Deinococcus radiodurans protein
  • Tn5 transposase active site contains the DDE motif which catalyzes the movement of the transposon[4].
  • Tn7 transposase is bacterial and highly specific[5].
  • Mos1 transposase mediates the movement of Mos1 transposon[6]
  • Tc3 transposase mediates the movement of Tc3 transposon in C. elegans[7]
  • Sleeping beauty transposase synthetic transposon developed as a non-viral vector for gene therapy[8]

Structural highlights

(PDB code 3ecp). Transposase contains a [9] enabling it to coordinate the binding of divalent metal ions. The metal ions affect transposase reactivity. The DDE motif is conserved in transposases and retroviral integrases and is essential for their activity.

3D structures of transposase

Transposase 3D structures


Structure of Tn5 transposase complex with DNA and glycerol (PDB code 3ecp).

Drag the structure with the mouse to rotate

ReferencesReferences

  1. ↑ Ivics Z, Li MA, Mates L, Boeke JD, Nagy A, Bradley A, Izsvak Z. Transposon-mediated genome manipulation in vertebrates. Nat Methods. 2009 Jun;6(6):415-22. doi: 10.1038/nmeth.1332. PMID:19478801 doi:http://dx.doi.org/10.1038/nmeth.1332
  2. ↑ Rice P, Mizuuchi K. Structure of the bacteriophage Mu transposase core: a common structural motif for DNA transposition and retroviral integration. Cell. 1995 Jul 28;82(2):209-20. PMID:7628012
  3. ↑ Park JM, Evertts AG, Levin HL. The Hermes transposon of Musca domestica and its use as a mutagen of Schizosaccharomyces pombe. Methods. 2009 Nov;49(3):243-7. doi: 10.1016/j.ymeth.2009.05.004. Epub 2009 May, 18. PMID:19450689 doi:http://dx.doi.org/10.1016/j.ymeth.2009.05.004
  4. ↑ Reznikoff WS. Transposon Tn5. Annu Rev Genet. 2008;42:269-86. PMID:18680433 doi:http://dx.doi.org/10.1146/annurev.genet.42.110807.091656
  5. ↑ Craig NL. Tn7: a target site-specific transposon. Mol Microbiol. 1991 Nov;5(11):2569-73. PMID:1664019
  6. ↑ Wang W, Swevers L, Iatrou K. Mariner (Mos1) transposase and genomic integration of foreign gene sequences in Bombyx mori cells. Insect Mol Biol. 2000 Apr;9(2):145-55. PMID:10762422
  7. ↑ Colloms SD, van Luenen HG, Plasterk RH. DNA binding activities of the Caenorhabditis elegans Tc3 transposase. Nucleic Acids Res. 1994 Dec 25;22(25):5548-54. PMID:7838706
  8. ↑ Ivics Z, Kaufman CD, Zayed H, Miskey C, Walisko O, Izsvak Z. The Sleeping Beauty transposable element: evolution, regulation and genetic applications. Curr Issues Mol Biol. 2004 Jan;6(1):43-55. PMID:14632258
  9. ↑ Klenchin VA, Czyz A, Goryshin IY, Gradman R, Lovell S, Rayment I, Reznikoff WS. Phosphate coordination and movement of DNA in the Tn5 synaptic complex: role of the (R)YREK motif. Nucleic Acids Res. 2008 Oct;36(18):5855-62. Epub 2008 Sep 12. PMID:18790806 doi:10.1093/nar/gkn577

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