Cargando…
The structure and function of an RNA polymerase interaction domain in the PcrA/UvrD helicase
The PcrA/UvrD helicase functions in multiple pathways that promote bacterial genome stability including the suppression of conflicts between replication and transcription and facilitating the repair of transcribed DNA. The reported ability of PcrA/UvrD to bind and backtrack RNA polymerase (1,2) migh...
Autores principales: | Sanders, Kelly, Lin, Chia-Liang, Smith, Abigail J., Cronin, Nora, Fisher, Gemma, Eftychidis, Vasileios, McGlynn, Peter, Savery, Nigel J., Wigley, Dale B., Dillingham, Mark S. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2017
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5397179/ https://www.ncbi.nlm.nih.gov/pubmed/28160601 http://dx.doi.org/10.1093/nar/gkx074 |
Ejemplares similares
-
The Conserved C-Terminus of the PcrA/UvrD Helicase Interacts Directly with RNA Polymerase
por: Gwynn, Emma J., et al.
Publicado: (2013) -
Analysis of the PcrA-RNA polymerase complex reveals a helicase interaction motif and a role for PcrA/UvrD helicase in the suppression of R-loops
por: Urrutia-Irazabal, Inigo, et al.
Publicado: (2021) -
Direct removal of RNA polymerase barriers to replication by accessory replicative helicases
por: Hawkins, Michelle, et al.
Publicado: (2019) -
The unstructured C-terminal extension of UvrD interacts with UvrB, but is dispensable for nucleotide excision repair
por: Manelyte, Laura, et al.
Publicado: (2009) -
UvrD helicase–RNA polymerase interactions are governed by UvrD’s carboxy-terminal Tudor domain
por: Kawale, Ashish A., et al.
Publicado: (2020)