Your browser doesn't support javascript.
loading
Mostrar: 20 | 50 | 100
Resultados 1 - 1 de 1
Filtrar
Mais filtros










Base de dados
Intervalo de ano de publicação
1.
J Mol Biol ; 436(11): 168589, 2024 Jun 01.
Artigo em Inglês | MEDLINE | ID: mdl-38677494

RESUMO

UvrD is a helicase vital for DNA replication and quality control processes. In its monomeric state, UvrD exhibits limited helicase activity, necessitating either dimerization or assistance from an accessory protein to efficiently unwind DNA. Within the DNA mismatch repair pathway, MutL plays a pivotal role in relaying the repair signal, enabling UvrD to unwind DNA from the strand incision site up to and beyond the mismatch. Although this interdependence is well-established, the precise mechanism of activation and the specific MutL-UvrD interactions that trigger helicase activity remain elusive. To address these questions, we employed site-specific crosslinking techniques using single-cysteine variants of MutL and UvrD followed by functional assays. Our investigation unveils that the C-terminal domain of MutL not only engages with UvrD but also acts as a self-sufficient activator of UvrD helicase activity on DNA substrates with 3'-single-stranded tails. Especially when MutL is covalently attached to the 2B or 1B domain the tail length can be reduced to a minimal substrate of 5 nucleotides without affecting unwinding efficiency.


Assuntos
DNA Helicases , Proteínas MutL , DNA/química , DNA Helicases/química , DNA Helicases/genética , Proteínas MutL/química , Proteínas MutL/genética , Ligação Proteica , Domínios Proteicos , Mesilatos/química , Reagentes de Ligações Cruzadas/química
SELEÇÃO DE REFERÊNCIAS
DETALHE DA PESQUISA
...