A5023533219- Bacterial Genetics and Biotechnology
- Enzyme Structure and Function
- RNA and protein synthesis mechanisms
- Protein Structure and Dynamics
- Bacteriophages and microbial interactions
- Lung Cancer Research Studies
- Metalloenzymes and iron-sulfur proteins
- Workplace Health and Well-being
- Congenital heart defects research
- Neurofibromatosis and Schwannoma Cases
- Heat shock proteins research
- Meningioma and schwannoma management
- Calpain Protease Function and Regulation
- Hemispheric Asymmetry in Neuroscience
- Paraquat toxicity studies and treatments
- Occupational Health and Safety Research
- Pharmacological Receptor Mechanisms and Effects
- Endoplasmic Reticulum Stress and Disease
- Genetics, Aging, and Longevity in Model Organisms
- Medical Research and Treatments
- Pesticide and Herbicide Environmental Studies
- Glioma Diagnosis and Treatment
- Electron Spin Resonance Studies
Gifu University
2025
Kyoto University
2021-2023
Kyoto Prefectural University of Medicine
2005
Veterans Health Administration
1996
The membrane-bound AAA protease FtsH is the key player controlling protein quality in bacteria. Two single-pass membrane proteins, HflK and HflC, interact with to modulate its proteolytic activity. Here, we present structure of entire FtsH-HflKC complex, comprising 12 copies both all which reciprocally form a cage, as well four hexamers periplasmic domains transmembrane helices enclosed inside cage cytoplasmic situated at base cage. K61/D62/S63 β2-β3 loop domain directly HflK, contributing...
TonB-dependent signal transduction is a versatile mechanism observed in gram-negative bacteria, integrating energy-dependent substrate transport with relay. In Escherichia coli, the TonB-ExbBD motor complex energizes transporter FecA, facilitating ferric citrate import. FecA also functions as sensor, transmitting signals to cytoplasmic membrane protein FecR. We previously demonstrated that FecR undergoes three-step cleavage process, culminating activation of sigma factor FecI, which drives...
TonB-dependent signal transduction is a versatile mechanism observed in gram-negative bacteria that integrates energy-dependent substrate transport with relay. In Escherichia coli , the TonB–ExbBD motor complex energizes outer membrane transporter FecA, facilitating ferric citrate import. FecA also acts as sensor, transmitting signals to cytoplasmic protein FecR, which eventually activates sigma factor FecI, driving transcription of fec operon. Building on our previous finding FecR undergoes...
Tumor necrosis factor-alpha (TNF-alpha) is a proinflammatory cytokine that elaborated in myriad of cardiac disease states. Although the biological role for TNF-alpha adult heart not known, recent study fetal myocardial cells has shown this increases synthesis low-molecular-weight stress proteins. These findings suggested interesting possibility might play functional by increasing expression proteins myocytes. Accordingly, purpose was to determine whether would modulate heat shock protein 72...
Site-2 proteases are a conserved family of intramembrane that cleave transmembrane substrates to regulate signal transduction and maintain proteostasis. Here, we elucidated crystal structures inhibitor-bound forms bacterial site-2 including Escherichia coli RseP. Structure-based chemical modification cross-linking experiments indicated the RseP domains surrounding active center undergo conformational changes expose substrate-binding site, suggesting has gating mechanism substrate entry....
Escherichia coli RseP, a member of the site-2 protease family intramembrane proteases, is involved in activation σE extracytoplasmic stress response and elimination signal peptides from cytoplasmic membrane. However, whether RseP has additional cellular functions unclear. In this study, we used mass spectrometry-based quantitative proteomic analysis to search for new substrates that might reveal unknown physiological roles RseP. Our data showed levels several Fec system proteins encoded by...
ABSTRACT The site2 - protease (S2P) family of intramembrane proteases (IMPs) is conserved in all kingdoms life and cleaves transmembrane proteins within the membrane to regulate maintain various cellular activities. RseP, an Escherichia coli S2P peptidase, involved regulation gene expression through regulated cleavage two target (RseA FecR) quality control proteolytic elimination remnant signal peptides. RseP expected have additional substrates be other processes. Recent studies shown that...
Abstract Site-2 proteases are a conserved family of intramembrane that cleave transmembrane substrates to regulate signal transduction and maintain proteostasis. Here, we elucidated crystal structures inhibitor-bound forms bacterial site-2 including E. coli RseP. Our observations consistent with rearrangement the RseP domains surrounding active center expose substrate-binding site where electrostatic linkage between membrane-associated mediates conformational changes, suggesting has gating...
Abstract Escherichia coli RseP, a member of the S2P family intramembrane proteases, is involved in activation σ E extracytoplasmic stress response and elimination remnant signal peptides. However, whether RseP has additional cellular functions unclear. In this study, we attempted to identify new substrates explore still unknown physiological roles protease. Our mass spectrometry-based quantitative proteomic analysis revealed that levels several Fec system proteins encoded by fecABCDE operon...