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

Francisco Tenjo-Castaño, Nicholas Sofos, Blanca López-Méndez, Luisa S. Stutzke, Anders Fuglsang, Stefano Stella and Guillermo Montoya ()
Additional contact information
Francisco Tenjo-Castaño: Faculty of Health and Medical Sciences University of Copenhagen
Nicholas Sofos: Faculty of Health and Medical Sciences University of Copenhagen
Blanca López-Méndez: Faculty of Health and Medical Sciences University of Copenhagen
Luisa S. Stutzke: Faculty of Health and Medical Sciences University of Copenhagen
Anders Fuglsang: Faculty of Health and Medical Sciences University of Copenhagen
Stefano Stella: Faculty of Health and Medical Sciences University of Copenhagen
Guillermo Montoya: Faculty of Health and Medical Sciences University of Copenhagen

Nature Communications, 2022, vol. 13, issue 1, 1-14

Abstract: 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 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.

Date: 2022
References: View references in EconPapers View complete reference list from CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/s41467-022-33504-5 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-33504-5

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-022-33504-5

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().