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Article

THAP9 transposase cleaves DNA via conserved acidic residues in an RNaseH-like domain

2021-03-17

Abstract excerpt

<title>Abstract</title> <p>Background: The catalytic domain of most ‘cut and paste’ DNA transposases have the canonical RNase-H fold which is also shared by other polynucleotidyl transferases like the retroviral integrases and the RAG1 subunit of V(D)J recombinase. The RNase-H fold is a mixture of beta sheets and alpha helices with three acidic residues (Asp, Asp, Glu/Asp - DDE/D) that are involved in the metal-m...

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Literature Corpus work
fda77b42-1174-599f-9199-5c5692e25e6b
DOI
10.21203/rs.3.rs-299079/v1
Open publication

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THAP9 transposase cleaves DNA via conserved acidic residues in an RNaseH-like domainDOI 10.21203/rs.3.rs-299079/v1
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