RESUMO
J proteins are obligate co-chaperones of Hsp70s. Via their signature J domain, all J proteins interact with their partner Hsp70s and stimulate their weak ATPase activity, which is vital for Hsp70 functions. The dependency of J proteins on their J domain is such that mutations in critical amino acids in the J domain often results into a null phenotype for a particular J protein. Here, we show that the J domain of Djp1, a cytosolic J protein important for peroxisomal protein import in Saccharomyces cerevisiae, is partially dispensable. A complete deletion of Djp1 J domain resulted into only partial loss in peroxisomal protein import function. Instead, the C-terminal domain of Djp1 was found to be essential for proper localization of the peroxisomal targeted GFP-PTS1. Furthermore, we show that Caj1, another cytosolic J protein, also has some role in peroxisomal protein import. Caj1 was found to be partially redundant with Djp1 as cells lacking both Djp1 and Caj1 resulted into a much more severe defect in GFP-PTS1 localization. Based on these results, we propose that dispensability of J domains could be attributed to genetic redundancy between different J proteins sharing common structural topology and cellular localization.
Assuntos
Proteínas de Ligação a Calmodulina/metabolismo , Proteínas de Choque Térmico HSP40/metabolismo , Chaperonas Moleculares/metabolismo , Peroxissomos/metabolismo , Proteínas de Saccharomyces cerevisiae/metabolismo , Saccharomyces cerevisiae/metabolismo , Proteínas de Ligação a Calmodulina/química , Proteínas de Ligação a Calmodulina/genética , Proteínas de Fluorescência Verde/genética , Proteínas de Fluorescência Verde/metabolismo , Proteínas de Choque Térmico HSP40/química , Proteínas de Choque Térmico HSP40/genética , Microscopia de Fluorescência , Chaperonas Moleculares/química , Chaperonas Moleculares/genética , Fator 1 de Elongação de Peptídeos/genética , Sinais de Orientação para Peroxissomos/genética , Fenótipo , Plasmídeos/genética , Plasmídeos/metabolismo , Domínios Proteicos , Transporte Proteico , Proteínas de Saccharomyces cerevisiae/química , Proteínas de Saccharomyces cerevisiae/genéticaRESUMO
AIM: To evaluate and compare the antimicrobial properties of propolis and calcium hydroxide alone and in combination with ciprofloxacin and moxifloxacin against Enterococcus faecalis (E. Faecalis). MATERIALS AND METHODS: The laboratory study was carried out to test the effectiveness of propolis and calcium hydroxidealone as well as in combination with the established endodontic medicaments (moxifloxacin and ciprofloxacin). The various combinations were-group 1: propolis, group 2: calcium hydroxide, group 3: moxifloxacin, group 4: ciprofoxacin, group 5: propolis + moxifloxacin, group 6: propolis + Ciprofloxacin, group 7: calcium hydroxide + ciprofloxacin, group 8: calcium hydroxide + moxifloxacin. The efficacy of these medicaments was tested by checking for the zone of inhibition for the specific strain (ATCC 29212) of E. faecalis at different time intervals, i.e. 24, 48 and 72 hours. RESULTS: Mean zone of inhibition was maximum in group V (21.94 ± 4.26) followed by group VI (18.80 ± 1.93), group I (18.71 ± 4.26), group VIII (15.88 ± 2.59), group III (14.91 ± 1.00), group VII (14.57 ± 2.17), group IV (13.91 ± 1.00) and minimum in group II (12.89 ± 2.14). Mean zone of inhibition was found to be maximum at 72 hours and minimum at 24 hours. At all time intervals, the combination of Propalis with Moxifocacin showed the maximum antimicrobial efficacy. CONCLUSION: On the basis of the results of the present study, it can be concluded that propolis and calcium hydroxide show synergistic effect with moxifloxacin and ciprofloxacin against E. Faecalis. Propolis in combination with antibiotics and alone is more effective than calcium hydroxide. CLINICAL SIGNIFICANCE: Since propolis alone and in combination with antibiotics was observed to be more effective than calcium hydroxide, propolis can be considered as an intracanal medicament when compared to traditional calcium hydroxide.
