Cargando…
Functional and structural similarity of human DNA primase [4Fe4S] cluster domain constructs
The regulatory subunit of human DNA primase has a C-terminal domain (p58C) that contains a [4Fe4S] cluster and binds DNA. Previous electrochemical analysis of a p58C construct revealed that its affinity for DNA is sensitive to the redox state of the [4Fe4S] cluster. Concerns about the validity of th...
Autores principales: | Holt, Marilyn E., Salay, Lauren E., O’Brien, Elizabeth, Barton, Jacqueline K., Chazin, Walter J. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2018
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6298731/ https://www.ncbi.nlm.nih.gov/pubmed/30562384 http://dx.doi.org/10.1371/journal.pone.0209345 |
Ejemplares similares
-
Yeast require redox switching in DNA primase
por: O’Brien, Elizabeth, et al.
Publicado: (2018) -
Flexibility and distributive synthesis regulate RNA priming and handoff in human DNA polymerase α-primase
por: Cordoba, John J., et al.
Publicado: (2023) -
Primer synthesis by a eukaryotic-like archaeal primase is independent of its Fe-S cluster
por: Holzer, Sandro, et al.
Publicado: (2017) -
Residues located in the primase domain of the bacteriophage T7 primase-helicase are essential for loading the hexameric complex onto DNA
por: Hernandez, Alfredo J., et al.
Publicado: (2022) -
DNA-Mediated
Signaling by Proteins with 4Fe–4S
Clusters Is Necessary for Genomic Integrity
por: Grodick, Michael A., et al.
Publicado: (2014)