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 />
 
 
}}


== References ==
== References ==

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky