Cargando…
Degradation of MinD oscillator complexes by Escherichia coli ClpXP
MinD is a cell division ATPase in Escherichia coli that oscillates from pole to pole and regulates the spatial position of the cell division machinery. Together with MinC and MinE, the Min system restricts assembly of the FtsZ-ring to midcell, oscillating between the opposite ends of the cell and pr...
Autores principales: | LaBreck, Christopher J., Trebino, Catherine E., Ferreira, Colby N., Morrison, Josiah J., DiBiasio, Eric C., Conti, Joseph, Camberg, Jodi L. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Society for Biochemistry and Molecular Biology
2020
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7857489/ https://www.ncbi.nlm.nih.gov/pubmed/33288679 http://dx.doi.org/10.1074/jbc.RA120.013866 |
Ejemplares similares
-
Degradation of the E. coli antitoxin MqsA by the proteolytic complex ClpXP is regulated by zinc occupancy and oxidation
por: Vos, Margaret R., et al.
Publicado: (2021) -
The Stress-Active Cell Division Protein ZapE Alters FtsZ Filament Architecture to Facilitate Division in Escherichia coli
por: DiBiasio, Eric C., et al.
Publicado: (2021) -
Regulation of Antimycin Biosynthesis Is Controlled by the ClpXP Protease
por: Bilyk, Bohdan, et al.
Publicado: (2020) -
The Protein Chaperone ClpX Targets Native and Non-native Aggregated Substrates for Remodeling, Disassembly, and Degradation with ClpP
por: LaBreck, Christopher J., et al.
Publicado: (2017) -
Location of Dual Sites in E. coli FtsZ Important for Degradation by ClpXP; One at the C-Terminus and One in the Disordered Linker
por: Camberg, Jodi L., et al.
Publicado: (2014)