Cargando…
Prokaryotic ubiquitin-like protein remains intrinsically disordered when covalently attached to proteasomal target proteins
BACKGROUND: The post-translational modification pathway referred to as pupylation marks proteins for proteasomal degradation in Mycobacterium tuberculosis and other actinobacteria by covalently attaching the small protein Pup (prokaryotic ubiquitin-like protein) to target lysine residues. In contras...
Autores principales: | Barandun, Jonas, Damberger, Fred F., Delley, Cyrille L., Laederach, Juerg, Allain, Frédéric H. T., Weber-Ban, Eilika |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2017
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5286830/ https://www.ncbi.nlm.nih.gov/pubmed/28143508 http://dx.doi.org/10.1186/s12900-017-0072-1 |
Ejemplares similares
-
Bacterial Proteasome Activator Bpa (Rv3780) Is a Novel Ring-Shaped Interactor of the Mycobacterial Proteasome
por: Delley, Cyrille L., et al.
Publicado: (2014) -
Electrostatic interactions guide substrate recognition of the prokaryotic ubiquitin-like protein ligase PafA
por: Block, Matthias F., et al.
Publicado: (2023) -
Pupylated proteins are subject to broad proteasomal degradation specificity and differential depupylation
por: Laederach, Juerg, et al.
Publicado: (2019) -
Structural basis of prokaryotic ubiquitin-like protein engagement and translocation by the mycobacterial Mpa-proteasome complex
por: Kavalchuk, Mikhail, et al.
Publicado: (2022) -
The pupylation pathway and its role in mycobacteria
por: Barandun, Jonas, et al.
Publicado: (2012)