The Interplay between Two Transcriptional Repressors and Chaperones Orchestrates Helicobacter pylori Heat-Shock Response.

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Annotation Summary

Term Occurence Count Dictionary
chloramphenicol 1 infectiousdiseasesdrugs
cholera 1 infectiousdiseases
pneumonia 1 infectiousdiseases
trachoma 2 infectiousdiseases
tuberculosis 2 infectiousdiseases

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Select Drug Character Offset Drug Term Instance
chloramphenicol 14056 affects bacterial HSP expression. Moreover, exposure of H. pylori cells to antibiotics, like kanamycin or chloramphenicol , leads to HspR downregulation, while HrcA expression was slightly affected only by kanamycin treatment
Select Disease Character Offset Disease Term Instance
cholera 6860 is widely distributed among bacteria, including pathogenic and opportunistic bacteria, like Vibrio cholera e and Pseudomonas aeruginosa [[16],[17]], although the model organism, Escherichia coli, where the heat-shock
pneumonia 7782 by dedicated transcriptional repressors, including clinically-relevant pathogens, like Streptococcus pneumonia e, Micoplasma genitalium, and Clostridium difficile [[19],[20],[21]]. The analysis of the H. pylori genome
trachoma 16023 transcriptional repressors have been described in different bacterial species, including B. subtilis, Chlamydia trachoma tis, S. coelicolor, and Mycobacterium tuberculosis [[35],[36],[37],[38]]. In these systems, chaperone
trachoma 17397 observation that is in line with the GroE-HrcA functional interaction characterized in B. subtilis and C. trachoma tis among the others [[35],[36]]. According to the “titration model” proposed for B. subtilis, upon
tuberculosis 16069 different bacterial species, including B. subtilis, Chlamydia trachomatis, S. coelicolor, and Mycobacterium tuberculosis [[35],[36],[37],[38]]. In these systems, chaperone proteins modulate the DNA-binding capabilities of
tuberculosis 18216 by a chaperone protein feedback. Differently from what has been observed in S. coelicolor and in M. tuberculosis [[37],[38]], in H. pylori HspR DNA-binding activity is not affected by DnaK, but by the heat-shock protein

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