Cargando…

The SspB adaptor drives structural changes in the AAA+ ClpXP protease during ssrA-tagged substrate delivery

Energy-dependent protein degradation by the AAA+ ClpXP protease helps maintain protein homeostasis in bacteria and eukaryotic organelles of bacterial origin. In Escherichia coli and many other proteobacteria, the SspB adaptor assists ClpXP in degrading ssrA-tagged polypeptides produced as a conseque...

Descripción completa

Detalles Bibliográficos
Autores principales:	Ghanbarpour, Alireza, Fei, Xue, Baker, Tania A., Davis, Joseph H., Sauer, Robert T.
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	National Academy of Sciences 2023
Materias:	Biological Sciences
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9963277/ https://www.ncbi.nlm.nih.gov/pubmed/36730206 http://dx.doi.org/10.1073/pnas.2219044120

Ejemplares similares

Structural basis of ClpXP recognition and unfolding of ssrA-tagged substrates
por: Fei, Xue, et al.
Publicado: (2020)

A closed translocation channel in the substrate-free AAA+ ClpXP protease diminishes rogue degradation
por: Ghanbarpour, Alireza, et al.
Publicado: (2023)

A Uniform Benchmark for Testing SsrA-Derived Degrons in the Escherichia coli ClpXP Degradation Pathway
por: Klimecka, Maria Magdalena, et al.
Publicado: (2021)

Insight into the RssB-Mediated Recognition and Delivery of σ(s) to the AAA+ Protease, ClpXP
por: Micevski, Dimce, et al.
Publicado: (2020)

Regulation of Antimycin Biosynthesis Is Controlled by the ClpXP Protease
por: Bilyk, Bohdan, et al.
Publicado: (2020)

The AAA+ protease ClpXP can easily degrade a 3(1) and a 5(2)-knotted protein
por: Sivertsson, Elin M., et al.
Publicado: (2019)

The ClpXP protease is dispensable for degradation of unfolded proteins in Staphylococcus aureus
por: Stahlhut, Steen G., et al.
Publicado: (2017)

Structures of the ATP-fueled ClpXP proteolytic machine bound to protein substrate
por: Fei, Xue, et al.
Publicado: (2020)

Cryo-EM structure of the ClpXP protein degradation machinery
por: Gatsogiannis, C, et al.
Publicado: (2019)

The functional ClpXP protease of Chlamydia trachomatis requires distinct clpP genes from separate genetic loci
por: Pan, Stefan, et al.
Publicado: (2019)

The Bacterial ClpXP-ClpB Family Is Enriched with RNA-Binding Protein Complexes
por: Auburger, Georg, et al.
Publicado: (2022)

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)

Degradation of MinD oscillator complexes by Escherichia coli ClpXP
por: LaBreck, Christopher J., et al.
Publicado: (2020)

A Functional ClpXP Protease is Required for Induction of the Accessory Toxin Genes, tst, sed, and sec
por: Schelin, Jenny, et al.
Publicado: (2020)

The Mitochondrial Unfoldase-Peptidase Complex ClpXP Controls Bioenergetics Stress and Metastasis
por: Seo, Jae Ho, et al.
Publicado: (2016)

Functional cooperativity between the trigger factor chaperone and the ClpXP proteolytic complex
por: Rizzolo, Kamran, et al.
Publicado: (2021)

Intrinsic Dynamics of the ClpXP Proteolytic Machine Using Elastic Network Models
por: González-Paz, Lenin, et al.
Publicado: (2023)

Drosophila protease ClpXP specifically degrades DmLRPPRC1 controlling mitochondrial mRNA and translation
por: Matsushima, Yuichi, et al.
Publicado: (2017)

Loss of the ClpXP Protease Leads to Decreased Resistance to Cell-Envelope Targeting Antimicrobials in Bacillus anthracis Sterne
por: Zou, Lang, et al.
Publicado: (2021)

Temperature dependence of ssrA-tag mediated protein degradation
por: Purcell, Oliver, et al.
Publicado: (2012)

A split protease-E. coli ClpXP system quantifies protein–protein interactions in Escherichia coli cells
por: Wang, Shengchen, et al.
Publicado: (2021)

Small molecule inhibitors of the mitochondrial ClpXP protease possess cytostatic potential and re-sensitize chemo-resistant cancers
por: Meßner, Martina, et al.
Publicado: (2021)

Strain-Dependent Recognition of a Unique Degradation Motif by ClpXP in Streptococcus mutans
por: Jana, Biswanath, et al.
Publicado: (2016)

The Essential Role of ClpXP in Caulobacter crescentus Requires Species Constrained Substrate Specificity
por: Vass, Robert H., et al.
Publicado: (2017)

The Mouse Heart Mitochondria N Terminome Provides Insights into ClpXP-Mediated Proteolysis
por: Hofsetz, Eduard, et al.
Publicado: (2020)

ClpXP and ClpAP proteolytic activity on divisome substrates is differentially regulated following the Caulobacter asymmetric cell division
por: Williams, Brandon, et al.
Publicado: (2014)

ClpXP protease targets long-lived DNA translocation states of a helicase-like motor to cause restriction alleviation
por: Simons, Michelle, et al.
Publicado: (2014)

NOA1, a Novel ClpXP Substrate, Takes an Unexpected Nuclear Detour Prior to Mitochondrial Import
por: Al-Furoukh, Natalie, et al.
Publicado: (2014)

Structural basis for inhibition of a response regulator of σ(S) stability by a ClpXP antiadaptor
por: Dorich, Victoria, et al.
Publicado: (2019)

A processive rotary mechanism couples substrate unfolding and proteolysis in the ClpXP degradation machinery
por: Ripstein, Zev A, et al.
Publicado: (2020)

Author Correction: Functional cooperativity between the trigger factor chaperone and the ClpXP proteolytic complex
por: Rizzolo, Kamran, et al.
Publicado: (2021)

Tailored Phenyl Esters Inhibit ClpXP and Attenuate Staphylococcus aureus α‐Hemolysin Secretion
por: Schwarz, Markus, et al.
Publicado: (2022)

Modular and coordinated activity of AAA+ active sites in the double-ring ClpA unfoldase of the ClpAP protease
por: Zuromski, Kristin L., et al.
Publicado: (2020)

AAA+ protease-adaptor structures reveal altered conformations and ring specialization
por: Kim, Sora, et al.
Publicado: (2022)

Optimization of ClpXP activity and protein synthesis in an E. coli extract-based cell-free expression system
por: Shi, Xinying, et al.
Publicado: (2018)

Insights into ClpXP proteolysis: heterooligomerization and partial deactivation enhance chaperone affinity and substrate turnover in Listeria monocytogenes
por: Balogh, Dóra, et al.
Publicado: (2017)

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)

A-Site mRNA Cleavage Is Not Required for tmRNA-Mediated ssrA-Peptide Tagging
por: Janssen, Brian D., et al.
Publicado: (2013)

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)

Inducible Synthetic Growth Regulation Using the ClpXP Proteasome Enhances cis,cis-Muconic Acid and Glycolic Acid Yields in Saccharomyces cerevisiae
por: Kakko, Natalia, et al.
Publicado: (2023)

Cannot write session to /tmp/vufind_sessions/sess_2qp8m1cua4kmunf7lm27tk07tt