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AAA+ ATPase

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https://www.readbyqxmd.com/read/28819163/fusion-protein-analysis-reveals-the-precise-regulation-between-hsp70-and-hsp100-during-protein-disaggregation
#1
Sayaka Hayashi, Yosuke Nakazaki, Kei Kagii, Hiromi Imamura, Yo-Hei Watanabe
ClpB, a bacterial Hsp100, is a ring-shaped AAA+ chaperone that can reactivate aggregated proteins in cooperation with DnaK, a bacterial Hsp70, and its co-factors. ClpB subunits comprise two AAA+ modules with an interstitial rod-shaped M-domain. The M-domain regulates ClpB ATPase activity and interacts directly with the DnaK nucleotide-binding domain (NBD). Here, to clarify how these functions contribute to the disaggregation process, we constructed ClpB, DnaK, and aggregated YFP fusion proteins in various combinations...
August 17, 2017: Scientific Reports
https://www.readbyqxmd.com/read/28819009/the-aaa-atpase-p97-a-cellular-multitool
#2
REVIEW
Lasse Stach, Paul S Freemont
The AAA+ (ATPases associated with diverse cellular activities) ATPase p97 is essential to a wide range of cellular functions, including endoplasmic reticulum-associated degradation, membrane fusion, NF-κB (nuclear factor kappa-light-chain-enhancer of activated B cells) activation and chromatin-associated processes, which are regulated by ubiquitination. p97 acts downstream from ubiquitin signaling events and utilizes the energy from ATP hydrolysis to extract its substrate proteins from cellular structures or multiprotein complexes...
August 17, 2017: Biochemical Journal
https://www.readbyqxmd.com/read/28815021/toward-an-understanding-of-the-cdc48-p97-atpase
#3
REVIEW
Nicholas Bodnar, Tom Rapoport
A conserved AAA+ ATPase, called Cdc48 in yeast and p97 or VCP in metazoans, plays an essential role in many cellular processes by segregating polyubiquitinated proteins from complexes or membranes. For example, in endoplasmic reticulum (ER)-associated protein degradation (ERAD), Cdc48/p97 pulls polyubiquitinated, misfolded proteins out of the ER and transfers them to the proteasome. Cdc48/p97 consists of an N-terminal domain and two ATPase domains (D1 and D2). Six Cdc48 monomers form a double-ring structure surrounding a central pore...
2017: F1000Research
https://www.readbyqxmd.com/read/28814508/dynamic-functional-assembly-of-the-torsin-aaa-atpase-and-its-modulation-by-lap1
#4
Anna R Chase, Ethan Laudermilch, Jimin Wang, Hideki Shigematsu, Takeshi Yokoyama, Christian Schlieker
TorsinA is an essential AAA+ ATPase requiring LAP1 or LULL1 as cofactors. The dynamics of the Torsin/cofactor system remain poorly understood, with previous models invoking Torsin/cofactor assemblies with fixed stoichiometries. Here, we demonstrate that TorsinA assembles into homotypic oligomers in the presence of ATP. Torsin variants mutated at the 'back' interface disrupt homo-oligomerization but still show robust ATPase activity in the presence of its cofactors. These Torsin mutants are severely compromised in their ability to rescue nuclear envelope defects in Torsin-deficient cells, suggesting that TorsinA homo-oligomers play a key role in vivo Engagement of the oligomer by LAP1 triggers ATP hydrolysis and rapid complex disassembly...
August 16, 2017: Molecular Biology of the Cell
https://www.readbyqxmd.com/read/28807601/ubx-domain-containing-proteins-are-involved-in-lipid-homeostasis-and-stress-responses-in-pichia-pastoris
#5
Meng Zhang, Qilin Yu, Zhe Liu, Chen Liang, Biao Zhang, Mingchun Li
Ubiquitin regulatory X (UBX) domain-containing proteins constitute a family of proteins and are substrate adaptors of AAA ATPase Cdc48. UBX proteins can bind to the N-terminal region of Cdc48 to perform endoplasmic reticulum associated protein degradation (ERAD). In this study, we identified two UBX domain-containing proteins, Ubx1 and Ubx2, in Pichia pastoris and found that the two proteins could recover the growth defect of Saccharomyces cerevisiae in ubx2Δ. Our results revealed that Ubx1 and Ubx2 play critical roles in synthesis of unsaturated fatty acids by affecting Spt23...
August 11, 2017: International Journal of Biochemistry & Cell Biology
https://www.readbyqxmd.com/read/28798962/structural-pathway-of-regulated-substrate-transfer-and-threading-through-an-hsp100-disaggregase
#6
Célia Deville, Marta Carroni, Kamila B Franke, Maya Topf, Bernd Bukau, Axel Mogk, Helen R Saibil
Refolding aggregated proteins is essential in combating cellular proteotoxic stress. Together with Hsp70, Hsp100 chaperones, including Escherichia coli ClpB, form a powerful disaggregation machine that threads aggregated polypeptides through the central pore of tandem adenosine triphosphatase (ATPase) rings. To visualize protein disaggregation, we determined cryo-electron microscopy structures of inactive and substrate-bound ClpB in the presence of adenosine 5'-O-(3-thiotriphosphate), revealing closed AAA+ rings with a pronounced seam...
August 2017: Science Advances
https://www.readbyqxmd.com/read/28798233/the-atad2-bromodomain-binds-different-acetylation-marks-on-the-histone-h4-in-similar-fuzzy-complexes
#7
Cassiano Langini, Amedeo Caflisch, Andreas Vitalis
Bromodomains are protein modules adopting conserved helix-bundle folds. Some bromodomain-containing proteins, such as ATPase family AAA domain-containing protein 2 (ATAD2), isoform A, have attracted much interest because they are overexpressed in many types of cancer. Bromodomains bind to acetylated lysine residues on histone tails and thereby facilitate the reading of the histone code. Epigenetic regulators in general have been implicated as indicators, mediators, or causes of a large number of diseases and disorders...
August 10, 2017: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/28783150/katanin-spiral-and-ring-structures-shed-light-on-power-stroke-for-microtubule-severing
#8
Elena Zehr, Agnieszka Szyk, Grzegorz Piszczek, Ewa Szczesna, Xiaobing Zuo, Antonina Roll-Mecak
Microtubule-severing enzymes katanin, spastin and fidgetin are AAA ATPases important for the biogenesis and maintenance of complex microtubule arrays in axons, spindles and cilia. Because of a lack of known 3D structures for these enzymes, their mechanism of action has remained poorly understood. Here we report the X-ray crystal structure of the monomeric AAA katanin module from Caenorhabditis elegans and cryo-EM reconstructions of the hexamer in two conformations. The structures reveal an unexpected asymmetric arrangement of the AAA domains mediated by structural elements unique to microtubule-severing enzymes and critical for their function...
August 7, 2017: Nature Structural & Molecular Biology
https://www.readbyqxmd.com/read/28770209/aaa-machines-of-protein-destruction-in-mycobacteria
#9
REVIEW
Adnan Ali H Alhuwaider, David A Dougan
The bacterial cytosol is a complex mixture of macromolecules (proteins, DNA, and RNA), which collectively are responsible for an enormous array of cellular tasks. Proteins are central to most, if not all, of these tasks and as such their maintenance (commonly referred to as protein homeostasis or proteostasis) is vital for cell survival during normal and stressful conditions. The two key aspects of protein homeostasis are, (i) the correct folding and assembly of proteins (coupled with their delivery to the correct cellular location) and (ii) the timely removal of unwanted or damaged proteins from the cell, which are performed by molecular chaperones and proteases, respectively...
2017: Frontiers in Molecular Biosciences
https://www.readbyqxmd.com/read/28768697/a-novel-high-throughput-yeast-genetic-screen-for-factors-modifying-protein-levels-of-the-early-onset-torsion-dystonia-associated-variant-torsina%C3%AE-e
#10
Lucía F Zacchi, John C Dittmar, Michael J Mihalevic, Annette M Shewan, Benjamin L Schulz, Jeffrey L Brodsky, Kara A Bernstein
Dystonia is the third most common movement disorder, but its diagnosis and treatment remain challenging. One of the most severe types of Dystonia is Early-Onset Torsion Dystonia (EOTD). The best studied and validated EOTD-associated mutation, torsinAΔE, is a deletion of a C-terminal glutamate residue in the AAA+ ATPase, torsinA. TorsinA appears to be an Endoplasmic Reticulum (ER)/Nuclear Envelope chaperone with multiple roles in the secretory pathway and in determining subcellular architecture. Many functions are disabled in the torsinAΔE variant, and torsinAΔE is also less stable than wild-type torsinA and is a substrate for ER-associated degradation...
August 2, 2017: Disease Models & Mechanisms
https://www.readbyqxmd.com/read/28760999/exploiting-conformational-plasticity-in-the-aaa-protein-vcp-p97-to-modify-function
#11
Anne Kathrin Schütz, Enrico Rennella, Lewis E Kay
p97/VCP, a member of the AAA+ (ATPases associated with diverse cellular activities) family of proteins, is implicated in the etiology of a group of degenerative diseases affecting bone and muscle tissue as well as the central nervous system. Methyl-TROSY-based NMR studies have previously revealed how disease-causing mutations deregulate a subtle dynamic conformational equilibrium involving the N-terminal domain (NTD) with implications for the binding of certain adaptors, providing insight into how disease mutations lead to abnormal function...
July 31, 2017: Proceedings of the National Academy of Sciences of the United States of America
https://www.readbyqxmd.com/read/28752667/genetic-networks-controlled-by-the-bacterial-replication-initiator-and-transcription-factor-dnaa-in-bacillus-subtilis
#12
Tracy A Washington, Janet L Smith, Alan D Grossman
DnaA is the widely conserved bacterial AAA+ ATPase that functions as both the replication initiator and a transcription factor. In many organisms, DnaA controls expression of its own gene and likely several others during growth and in response to replication stress. To evaluate the effects of DnaA on gene expression, separate from its role in replication initiation, we analyzed changes in mRNA levels in Bacillus subtilis cells with and without dnaA, using engineered strains in which dnaA is not essential. We found that dnaA was required for many of the changes in gene expression in response to replication stress...
July 27, 2017: Molecular Microbiology
https://www.readbyqxmd.com/read/28747908/unraveling-rubisco-form-i-and-form-ii-regulation-in-an-uncultured-organism-from-a-deep-sea-hydrothermal-vent-via-metagenomic-and-mutagenesis-studies
#13
Stefanie Böhnke, Mirjam Perner
Ribulose-1,5-bisphosphate carboxylase/oxygenase (RubisCO) catalyzes the first major step of carbon fixation in the Calvin-Benson-Bassham (CBB) cycle. This autotrophic CO2 fixation cycle accounts for almost all the assimilated carbon on Earth. Due to the primary role that RubisCO plays in autotrophic carbon fixation, it is important to understand how its gene expression is regulated and the enzyme is activated. Since the majority of all microorganisms are currently not culturable, we used a metagenomic approach to identify genes and enzymes associated with RubisCO expression...
2017: Frontiers in Microbiology
https://www.readbyqxmd.com/read/28712723/msp1-is-a-membrane-protein-dislocase-for-tail-anchored-proteins
#14
Matthew L Wohlever, Agnieszka Mateja, Philip T McGilvray, Kasey J Day, Robert J Keenan
Mislocalized tail-anchored (TA) proteins of the outer mitochondrial membrane are cleared by a newly identified quality control pathway involving the conserved eukaryotic protein Msp1 (ATAD1 in humans). Msp1 is a transmembrane AAA-ATPase, but its role in TA protein clearance is not known. Here, using purified components reconstituted into proteoliposomes, we show that Msp1 is both necessary and sufficient to drive the ATP-dependent extraction of TA proteins from the membrane. A crystal structure of the Msp1 cytosolic region modeled into a ring hexamer suggests that active Msp1 contains a conserved membrane-facing surface adjacent to a central pore...
July 20, 2017: Molecular Cell
https://www.readbyqxmd.com/read/28710470/deviation-of-the-typical-aaa-substrate-threading-pore-prevents-fatal-protein-degradation-in-yeast-cdc48
#15
Masatoshi Esaki, Md Tanvir Islam, Naoki Tani, Teru Ogura
Yeast Cdc48 is a well-conserved, essential chaperone of ATPases associated with diverse cellular activity (AAA) proteins, which recognizes substrate proteins and modulates their conformations to carry out many cellular processes. However, the fundamental mechanisms underlying the diverse pivotal roles of Cdc48 remain unknown. Almost all AAA proteins form a ring-shaped structure with a conserved aromatic amino acid residue that is essential for proper function. The threading mechanism hypothesis suggests that this residue guides the intrusion of substrate proteins into a narrow pore of the AAA ring, thereby becoming unfolded...
July 14, 2017: Scientific Reports
https://www.readbyqxmd.com/read/28709027/singlet-oxygen-triggers-chloroplast-rupture-and-cell-death-in-the-zeaxanthin-epoxidase-defective-mutant-aba1-of-arabidopsis-thaliana-under-high-light-stress
#16
Álvaro Sánchez-Corrionero, Inmaculada Sánchez-Vicente, Sergio González-Pérez, Ascensión Corrales, Anja Krieger-Liszkay, Óscar Lorenzo, Juan B Arellano
The two Arabidopsis thaliana mutants, aba1 and max4, were previously identified as sharing a number of co-regulated genes with both the flu mutant and Arabidopsis cell suspension cultures exposed to high light (HL). On this basis, we investigated whether aba1 and max4 were generating high amounts of singlet oxygen ((1)O2) and activating (1)O2-mediated cell death. Thylakoids of aba1 produced twice as much (1)O2 as thylakoids of max4 and wild type (WT) plants when illuminated with strong red light. (1)O2 was measured using the spin probe 2,2,6,6-tetramethyl-4-piperidone hydrochloride...
September 2017: Journal of Plant Physiology
https://www.readbyqxmd.com/read/28704538/intestinal-calcium-and-bile-salts-facilitate-germination-of-clostridium-difficile-spores
#17
Travis J Kochan, Madeline J Somers, Alyssa M Kaiser, Michelle S Shoshiev, Ada K Hagan, Jessica L Hastie, Nicole P Giordano, Ashley D Smith, Alyxandria M Schubert, Paul E Carlson, Philip C Hanna
Clostridium difficile (C. difficile) is an anaerobic gram-positive pathogen that is the leading cause of nosocomial bacterial infection globally. C. difficile infection (CDI) typically occurs after ingestion of infectious spores by a patient that has been treated with broad-spectrum antibiotics. While CDI is a toxin-mediated disease, transmission and pathogenesis are dependent on the ability to produce viable spores. These spores must become metabolically active (germinate) in order to cause disease. C. difficile spore germination occurs when spores encounter bile salts and other co-germinants within the small intestine, however, the germination signaling cascade is unclear...
July 2017: PLoS Pathogens
https://www.readbyqxmd.com/read/28700685/characterization-of-the-molecular-chaperone-clpb-from-the-pathogenic-spirochaete-leptospira-interrogans
#18
Joanna Krajewska, Anna Modrak-Wójcik, Zbigniew J Arent, Daniel Więckowski, Michal Zolkiewski, Agnieszka Bzowska, Sabina Kędzierska-Mieszkowska
Leptospira interrogans is a spirochaete responsible for leptospirosis in mammals. The molecular mechanisms of the Leptospira virulence remain mostly unknown. Recently, it has been demonstrated that an AAA+ chaperone ClpB (a member of the Hsp100 family) from L. interrogans (ClpBLi) is not only essential for survival of Leptospira under the thermal and oxidative stresses, but also during infection of a host. The aim of this study was to provide further insight into the role of ClpB in the pathogenic spirochaetes and explore its biochemical properties...
2017: PloS One
https://www.readbyqxmd.com/read/28691899/aggregation-of-a-hepatitis-c-virus-replicase-module-induced-by-ablation-of-p97-vcp
#19
Zhigang Yi, Zhenghong Yuan
Hijacking host membranes to assemble a membrane-associated viral replicase is a hallmark of almost all positive-strand RNA viruses. However, how the virus co-opts host factors to facilitate this energy-unfavourable process is incompletely understood. In a previous study, using hepatitis C virus (HCV) as a model and employing affinity purification of the viral replicase, we identified a valosin-containing protein (p97/VCP), a member of the ATPases associated with diverse cellular activities (AAA+ ATPase family), as a viral replicase-associated host factor...
July 2017: Journal of General Virology
https://www.readbyqxmd.com/read/28689658/conformational-landscape-of-the-p28-bound-human-proteasome-regulatory-particle
#20
Ying Lu, Jiayi Wu, Yuanchen Dong, Shuobing Chen, Shuangwu Sun, Yong-Bei Ma, Qi Ouyang, Daniel Finley, Marc W Kirschner, Youdong Mao
The proteasome holoenzyme is activated by its regulatory particle (RP) consisting of two subcomplexes, the lid and the base. A key event in base assembly is the formation of a heterohexameric ring of AAA-ATPases, which is guided by at least four RP assembly chaperones in mammals: PAAF1, p28/gankyrin, p27/PSMD9, and S5b. Using cryogenic electron microscopy, we analyzed the non-AAA structure of the p28-bound human RP at 4.5 Å resolution and determined seven distinct conformations of the Rpn1-p28-AAA subcomplex within the p28-bound RP at subnanometer resolutions...
July 20, 2017: Molecular Cell
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