Results 1 to 10 of about 2,123 (100)

Molecular Characterization of the ClpC AAA+ ATPase in the Biology of Chlamydia trachomatis [PDF]

mBio, 2023
Bacterial AAA+ unfoldases are crucial for bacterial physiology by recognizing specific substrates and, typically, unfolding them for degradation by a proteolytic component. The caseinolytic protease (Clp) system is one example where a hexameric unfoldase
Stefan Pan, Aaron A. Jensen, Nicholas A. Wood, Beate Henrichfreise, Heike Brötz-Oesterhelt, Derek J. Fisher, Peter Sass, Scot P. Ouellette   +7 more
doaj   +4 more sources

Structure of the central Staphylococcus aureus AAA+ protease MecA/ClpC/ClpP [PDF]

Communications Biology
Bacterial AAA+ proteases are composed of a AAA+ partner (e.g., ClpC) and an associated peptidase (e.g., ClpP). They represent ATP-fuelled and self-compartmentalized proteolytic machines that are crucial for stress resistance and virulence.
Stavros Azinas, Karin Wallden, Panagiotis Katikaridis, Timo Jenne, Adrien Schahl, Axel Mogk, Marta Carroni   +6 more
doaj   +2 more sources

Allosteric control of the bacterial ClpC/ClpP protease and its hijacking by antibacterial peptides [PDF]

The EMBO Journal
The hexameric AAA+ protein ClpC, combined with peptidase ClpP, forms a critical ATP-dependent protease in bacteria, essential for virulence. ClpC is usually repressed in an inactive resting state, where two ClpC spirals interact via coiled-coil M-domains.
Timo Jenne, Lisa Engelhardt, Ieva Baronaite, Dorit Levy, Inbal Riven, Maciej Malolepszy, Stavros Azinas, Taras Sych, Erdinc Sezgin, Dirk Flemming, Irmgard Sinning, Gilad Haran, Marta Carroni, Axel Mogk   +13 more
doaj   +2 more sources

clpC-Mediated Translational Control Orchestrates Stress Tolerance and Biofilm Formation in Milk-Originated Staphylococcus aureus RMSA24 [PDF]

Foods
Staphylococcus aureus 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 S.
Maofeng Zhang, Jie Hu, Ting Xue
doaj   +2 more sources

Bioinformatic identification of ClpI, a distinct class of Clp unfoldases in Actinomycetota [PDF]

Frontiers in Microbiology, 2023
All clades of bacteria possess Hsp100/Clp family unfoldase enzymes that contribute to aspects of protein quality control. In Actinomycetota, these include ClpB, which functions as an independent chaperone and disaggregase, and ClpC, which cooperates with
Jialiu Jiang, Karl R. Schmitz, Karl R. Schmitz   +2 more
doaj   +2 more sources

Thioredoxin and its partner protein are essential for zoospore flagellar formation in Actinoplanes missouriensis [PDF]

Communications Biology
The filamentous bacterium Actinoplanes missouriensis produces flagellated spores, which become zoospores after release, in sporangia. However, the regulatory mechanism of spore flagellation remains unclear.
Tomohiro Kimura, Satoshi Maeda, Remi Suzuki, Takeaki Tezuka, Yasuo Ohnishi   +4 more
doaj   +2 more sources

Overexpressing the ClpC AAA+ unfoldase accelerates developmental cycle progression in Chlamydia trachomatis [PDF]

mBio
Chlamydia is an obligate intracellular bacterium that undergoes a complex biphasic developmental cycle, alternating between the smaller, infectious, non-dividing elementary body (EB) and the larger, non-infectious but dividing reticulate body. Due to the
Aaron A. Jensen, Saba Firdous, Lei Lei, Derek J. Fisher, Scot P. Ouellette   +4 more
doaj   +2 more sources

ApoE Mimetic Peptide COG1410 Kills Mycobacterium smegmatis via Directly Interfering ClpC’s ATPase Activity [PDF]

Antibiotics
Antimicrobial peptides (AMPs) hold promise as alternatives to combat bacterial infections, addressing the urgent global threat of antibiotic resistance.
Chun Wang, Yun-Yao Ren, Li-Mei Han, Peng-Cheng Yi, Wei-Xiao Wang, Cai-Yun Zhang, Xiu-Zhen Chen, Ming-Zhe Chi, Apeng Wang, Wei Chen, Chun-Mei Hu   +10 more
doaj   +2 more sources

Septic Shock Caused by Coinfection of Shewanella algae Bloodstream Infection and Epstein‐Barr Virus: Clinical Characteristics and Genomic Analysis [PDF]

MicrobiologyOpen
Shewanella algae, a marine‐origin opportunistic pathogen, has shown a significant increase in non‐coastal infections, yet its environmental adaptability and synergistic pathogenic mechanisms with Epstein‐Barr virus (EBV) coinfection remain unclear.
Jianmei Chen, Dong Ling, Feng Wang, Liping Liu, Yucheng Ren, Chengying Chen, Na Su   +6 more
doaj   +2 more sources

MecA in Streptococcus mutans is a multi-functional protein [PDF]

mSphere
Our recent studies have shown that deficiency of MecA in Streptococcus mutans significantly affects cell division, growth, and biofilm formation. In this study, an in vitro mixed-species model, proteomics, and affinity pull-down assays were used to ...
Kassapa Ellepola, Robert C. Shields, Jessica K. Kajfasz, Hua Zhang, Jose A. Lemos, Hui Wu, Zezhang T. Wen   +6 more
doaj   +2 more sources