Structure of the TnsB transposase-DNA complex of type V-K CRISPR-associated transposon

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Structure of the TnsB transposase-DNA complex of type V-K CRISPR-associated transposon. / Tenjo-Castaño, Francisco; Sofos, Nicholas; López-Méndez, Blanca; Stutzke, Luisa S.; Fuglsang, Anders; Stella, Stefano; Montoya, Guillermo.

In: Nature Communications, Vol. 13, 5792, 2022.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Tenjo-Castaño, F, Sofos, N, López-Méndez, B, Stutzke, LS, Fuglsang, A, Stella, S & Montoya, G 2022, 'Structure of the TnsB transposase-DNA complex of type V-K CRISPR-associated transposon', Nature Communications, vol. 13, 5792. https://doi.org/10.1038/s41467-022-33504-5

APA

Tenjo-Castaño, F., Sofos, N., López-Méndez, B., Stutzke, L. S., Fuglsang, A., Stella, S., & Montoya, G. (2022). Structure of the TnsB transposase-DNA complex of type V-K CRISPR-associated transposon. Nature Communications, 13, [5792]. https://doi.org/10.1038/s41467-022-33504-5

Vancouver

Tenjo-Castaño F, Sofos N, López-Méndez B, Stutzke LS, Fuglsang A, Stella S et al. Structure of the TnsB transposase-DNA complex of type V-K CRISPR-associated transposon. Nature Communications. 2022;13. 5792. https://doi.org/10.1038/s41467-022-33504-5

Author

Tenjo-Castaño, Francisco ; Sofos, Nicholas ; López-Méndez, Blanca ; Stutzke, Luisa S. ; Fuglsang, Anders ; Stella, Stefano ; Montoya, Guillermo. / Structure of the TnsB transposase-DNA complex of type V-K CRISPR-associated transposon. In: Nature Communications. 2022 ; Vol. 13.

Bibtex

@article{ca3c639226904bc1b8020a62089c2f0d,
title = "Structure of the TnsB transposase-DNA complex of type V-K CRISPR-associated transposon",
abstract = "CRISPR-associated transposons (CASTs) are mobile genetic elements that co-opted CRISPR-Cas systems for RNA-guided transposition. Here we present the 2.4 {\AA} cryo-EM structure of the Scytonema hofmannii (sh) TnsB transposase from Type V-K CAST, bound to the strand transfer DNA. The strand transfer complex displays an intertwined pseudo-symmetrical architecture. Two protomers involved in strand transfer display a catalytically competent active site composed by DDE residues, while other two, which play a key structural role, show active sites where the catalytic residues are not properly positioned for phosphodiester hydrolysis. Transposon end recognition is accomplished by the NTD1/2 helical domains. A singular in trans association of NTD1 domains of the catalytically competent subunits with the inactive DDE domains reinforces the assembly. Collectively, the structural features suggest that catalysis is coupled to protein-DNA assembly to secure proper DNA integration. DNA binding residue mutants reveal that lack of specificity decreases activity, but it could increase transposition in some cases. Our structure sheds light on the strand transfer reaction of DDE transposases and offers new insights into CAST transposition.",
author = "Francisco Tenjo-Casta{\~n}o and Nicholas Sofos and Blanca L{\'o}pez-M{\'e}ndez and Stutzke, {Luisa S.} and Anders Fuglsang and Stefano Stella and Guillermo Montoya",
note = "Publisher Copyright: {\textcopyright} 2022, The Author(s).",
year = "2022",
doi = "10.1038/s41467-022-33504-5",
language = "English",
volume = "13",
journal = "Nature Communications",
issn = "2041-1723",
publisher = "nature publishing group",

}

RIS

TY - JOUR

T1 - Structure of the TnsB transposase-DNA complex of type V-K CRISPR-associated transposon

AU - Tenjo-Castaño, Francisco

AU - Sofos, Nicholas

AU - López-Méndez, Blanca

AU - Stutzke, Luisa S.

AU - Fuglsang, Anders

AU - Stella, Stefano

AU - Montoya, Guillermo

N1 - Publisher Copyright: © 2022, The Author(s).

PY - 2022

Y1 - 2022

N2 - CRISPR-associated transposons (CASTs) are mobile genetic elements that co-opted CRISPR-Cas systems for RNA-guided transposition. Here we present the 2.4 Å cryo-EM structure of the Scytonema hofmannii (sh) TnsB transposase from Type V-K CAST, bound to the strand transfer DNA. The strand transfer complex displays an intertwined pseudo-symmetrical architecture. Two protomers involved in strand transfer display a catalytically competent active site composed by DDE residues, while other two, which play a key structural role, show active sites where the catalytic residues are not properly positioned for phosphodiester hydrolysis. Transposon end recognition is accomplished by the NTD1/2 helical domains. A singular in trans association of NTD1 domains of the catalytically competent subunits with the inactive DDE domains reinforces the assembly. Collectively, the structural features suggest that catalysis is coupled to protein-DNA assembly to secure proper DNA integration. DNA binding residue mutants reveal that lack of specificity decreases activity, but it could increase transposition in some cases. Our structure sheds light on the strand transfer reaction of DDE transposases and offers new insights into CAST transposition.

AB - CRISPR-associated transposons (CASTs) are mobile genetic elements that co-opted CRISPR-Cas systems for RNA-guided transposition. Here we present the 2.4 Å cryo-EM structure of the Scytonema hofmannii (sh) TnsB transposase from Type V-K CAST, bound to the strand transfer DNA. The strand transfer complex displays an intertwined pseudo-symmetrical architecture. Two protomers involved in strand transfer display a catalytically competent active site composed by DDE residues, while other two, which play a key structural role, show active sites where the catalytic residues are not properly positioned for phosphodiester hydrolysis. Transposon end recognition is accomplished by the NTD1/2 helical domains. A singular in trans association of NTD1 domains of the catalytically competent subunits with the inactive DDE domains reinforces the assembly. Collectively, the structural features suggest that catalysis is coupled to protein-DNA assembly to secure proper DNA integration. DNA binding residue mutants reveal that lack of specificity decreases activity, but it could increase transposition in some cases. Our structure sheds light on the strand transfer reaction of DDE transposases and offers new insights into CAST transposition.

U2 - 10.1038/s41467-022-33504-5

DO - 10.1038/s41467-022-33504-5

M3 - Journal article

C2 - 36184667

AN - SCOPUS:85139095440

VL - 13

JO - Nature Communications

JF - Nature Communications

SN - 2041-1723

M1 - 5792

ER -

ID: 322565421