RAD54 N-terminal domain is a DNA sensor that couples ATP hydrolysis with branch migration of Holliday junctions
RAD54 stimulates activity of the RAD51 recombinase and catalyzes branch migration of Holliday junctions during DNA repair and recombination. Here the authors show that the N-terminal domain of RAD54 mediates RAD54 oligomerization to promote branch migration, and is the target of phosphorylation that...
Enregistré dans:
Auteurs principaux: | Nadish Goyal, Matthew J. Rossi, Olga M. Mazina, Yong Chi, Robert L. Moritz, Bruce E. Clurman, Alexander V. Mazin |
---|---|
Format: | article |
Langue: | EN |
Publié: |
Nature Portfolio
2018
|
Sujets: | |
Accès en ligne: | https://doaj.org/article/b15bd6aeba5249c9abdcd8a19d96755d |
Tags: |
Ajouter un tag
Pas de tags, Soyez le premier à ajouter un tag!
|
Documents similaires
-
ATP hydrolysis by UPF1 is required for efficient translation termination at premature stop codons
par: Lucas D. Serdar, et autres
Publié: (2016) -
Targeted Therapy of Colon Cancer by Aptamer-Guided Holliday Junctions Loaded with Doxorubicin
par: Yao F, et autres
Publié: (2020) -
Structural insights into sequence-dependent Holliday junction resolution by the chloroplast resolvase MOC1
par: Junjie Yan, et autres
Publié: (2020) -
RuvC uses dynamic probing of the Holliday junction to achieve sequence specificity and efficient resolution
par: Karolina Maria Górecka, et autres
Publié: (2019) -
Replication intermediates that escape Dna2 activity are processed by Holliday junction resolvase Yen1
par: Gizem Ölmezer, et autres
Publié: (2016)