Cargando…
Insight into the RssB-Mediated Recognition and Delivery of σ(s) to the AAA+ Protease, ClpXP
In Escherichia coli, SigmaS (σ(S)) is the master regulator of the general stress response. The cellular levels of σ(S) are controlled by transcription, translation and protein stability. The turnover of σ(S), by the AAA+ protease (ClpXP), is tightly regulated by a dedicated adaptor protein, termed R...
Autores principales: | Micevski, Dimce, Zeth, Kornelius, Mulhern, Terrence D., Schuenemann, Verena J., Zammit, Jessica E., Truscott, Kaye N., Dougan, David A. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2020
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7226468/ https://www.ncbi.nlm.nih.gov/pubmed/32316259 http://dx.doi.org/10.3390/biom10040615 |
Ejemplares similares
-
Anti-adaptors use distinct modes of binding to inhibit the RssB-dependent turnover of RpoS (σ(S)) by ClpXP
por: Micevski, Dimce, et al.
Publicado: (2015) -
Polymerase delta-interacting protein 38 (PDIP38) modulates the stability and activity of the mitochondrial AAA+ protease CLPXP
por: Strack, Philip R., et al.
Publicado: (2020) -
Structural basis for inhibition of a response regulator of σ(S) stability by a ClpXP antiadaptor
por: Dorich, Victoria, et al.
Publicado: (2019) -
A closed translocation channel in the substrate-free AAA+ ClpXP protease diminishes rogue degradation
por: Ghanbarpour, Alireza, et al.
Publicado: (2023) -
Regulation of Antimycin Biosynthesis Is Controlled by the ClpXP Protease
por: Bilyk, Bohdan, et al.
Publicado: (2020)