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TitleIS21 family transposase cleaved donor complex traps two right-handed superhelical crossings.
Journal, issue, pagesNat Commun, Vol. 14, Issue 1, Page 2335, Year 2023
Publish dateApr 22, 2023
AuthorsMercedes Spínola-Amilibia / Lidia Araújo-Bazán / Álvaro de la Gándara / James M Berger / Ernesto Arias-Palomo /
PubMed AbstractTransposases are ubiquitous enzymes that catalyze DNA rearrangement events with broad impacts on gene expression, genome evolution, and the spread of drug-resistance in bacteria. Here, we use ...Transposases are ubiquitous enzymes that catalyze DNA rearrangement events with broad impacts on gene expression, genome evolution, and the spread of drug-resistance in bacteria. Here, we use biochemical and structural approaches to define the molecular determinants by which IstA, a transposase present in the widespread IS21 family of mobile elements, catalyzes efficient DNA transposition. Solution studies show that IstA engages the transposon terminal sequences to form a high-molecular weight complex and promote DNA integration. A 3.4 Å resolution structure of the transposase bound to transposon ends corroborates our biochemical findings and reveals that IstA self-assembles into a highly intertwined tetramer that synapses two supercoiled terminal inverted repeats. The three-dimensional organization of the IstA•DNA cleaved donor complex reveals remarkable similarities with retroviral integrases and classic transposase systems, such as Tn7 and bacteriophage Mu, and provides insights into IS21 transposition.
External linksNat Commun / PubMed:37087515 / PubMed Central
MethodsEM (single particle)
Resolution3.35 Å
Structure data

15848

8b4h

EMDB-15848, PDB-8b4h:
IstA transposase cleaved donor complex
Method: EM (single particle) / Resolution: 3.35 Å

Chemicals

ChemComp-MG:
Unknown entry

Source
  • geobacillus stearothermophilus (bacteria)
KeywordsDNA BINDING PROTEIN / DNA Transposition / Transposase / Cleaved donor complex / DDE domain / IS21 / IstA / Insertion sequence

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