HSP101 | ClpB heat shock protein, N_terminal
- Known as:
- HSP101 | ClpB heat shock protein, N_terminal
- Catalog number:
- AS08 283
- Product Quantity:
- 200 ul
- Category:
- -
- Supplier:
- Agris
- Gene target:
- HSP101 | ClpB heat shock protein N_terminal
Ask about this productRelated genes to: HSP101 | ClpB heat shock protein, N_terminal
- Gene:
- CLPB NIH gene
- Name:
- ClpB homolog, mitochondrial AAA ATPase chaperonin
- Previous symbol:
- -
- Synonyms:
- HSP78, SKD3, FLJ13152, ANKCLB
- Chromosome:
- 11q13.4
- Locus Type:
- gene with protein product
- Date approved:
- 2005-10-04
- Date modifiied:
- 2019-04-23
Related products to: HSP101 | ClpB heat shock protein, N_terminal
Related articles to: HSP101 | ClpB heat shock protein, N_terminal
- Protein quality control (PQC) systems are essential for cellular resilience to proteotoxic stress. Despite intensive study, functional redundancies in the system obscure the contributions of important individual genes. Here, we leverage transposon sequencing (Tn-seq) across bacterial strains lacking key chaperones and proteases to reveal hidden determinants of stress response in protein homeostasis. By profiling fitness under multiple proteotoxic stresses, we uncover stress-specific vulnerabilities and reveal how major players of PQC mask correlations between transcriptomic responses and gene fitness. We identify a heat-specific synthetic lethality between the ClpB disaggregase and DNA polymerase 1 mediated by prolific aggregation of the RecA recombinase and persistent induction of the heat shock regulon, supporting a conclusion that vulnerabilities in PQC are genetic- and environmental-context specific. Overall, our work presents a framework to reveal critical addressable fragilities in stress responses using gene fitness scores adaptable to a variety of systems. - Source: PubMed
Publication date: 2026/01/22
Aldikacti BerentPutun HidayetSarsani VishalZeinert RileeFlaherty PatrickChien Peter - How biological machines harness ATP to drive mechanical work remains a crucial question. Structural studies of protein-translocating AAA+ machines proposed a coupled and sequential translocation process, whereby ATP hydrolysis events lead to short threading steps. Yet, direct real-time observation of these events remains elusive. Here, we employ single-molecule FRET spectroscopy to track substrate translocation through ClpB, a quality control AAA+ machine. We isolate ClpB and its substrate within lipid vesicles and find that translocation events, while dependent on ATP, take milliseconds, much faster than ATP hydrolysis times. Surprisingly, the translocation rate depends weakly on temperature and ATP concentration. Using three-color FRET experiments, we find that translocation events can occur bidirectionally but are not always complete. Replacing ATP with the slowly hydrolysable analog ATPγS abolishes both rapid translocation and directionality. These results indicate a fast, stochastic Brownian-motor-like mechanism, redefining how ATP is coupled with mechanical action in AAA+ machines. - Source: PubMed
Publication date: 2026/01/21
Casier RemiLevy DoritRiven InbalBarak YoavHaran Gilad - Congenital neutropenia (CN) encompasses a group of disorders characterized by impaired neutrophil differentiation, resulting in persistently low neutrophil counts in the peripheral blood. It presents with recurrent infections and an elevated risk of leukemia. Multiple genetic mutations have been implicated in the pathogenesis of neutropenia. - Source: PubMed
Sun YuxingTang MinHe JuanHu XiaoqinLi MingTan Li - - Source: PubMed
Publication date: 2026/01/08
Fetissov Sergueï O - is an important pathogen that can cause widespread infections as well as severe outbreaks of food poisoning. Recent studies have drawn attention to foodborne pathogens such as endowed with the ability to form biofilms and increase resistance to antimicrobial agents as well as environmental stress, posing challenges to food safety. The Clp (caseinolytic protease) protein complex plays a crucial role in energy-dependent protein hydrolysis processes. This mechanism is a common way to maintain intracellular homeostasis and regulation in both prokaryotic and eukaryotic cells, especially under stress conditions. In , multiple genes encoding Clp ATPase homologues have been identified: , , , , and . This study investigated the roles of in stress tolerance and biofilm formation of foodborne RMSA24 isolated from raw milk. Our results showed that the deletion of the gene significantly reduced the bacterium's tolerance to heat, desiccation, hydrogen peroxide, and high osmotic pressure compared to wild type (WT). Furthermore, the knockout mutant also exhibited a marked decrease in biofilm formation using Crystal Violet Staining (CVS) and Scanning Electron Microscopy (SEM). Finally, compared to WT, there was a total of 102 DEGs (differentially expressed genes), with a significant downregulation of genes related to biofilm formation and ) and heat-shock response ( and ). These findings suggest that regulates environmental tolerance in by modulating the expression of stress- and biofilm-related genes, positioning it as a potential biomarker and a novel target for controlling contamination in the food industry. - Source: PubMed
Publication date: 2025/12/16
Zhang MaofengHu JieXue Ting