scholarly journals Further Characterization ofBacillus subtilisAntibiotic Biosensors and Their Use for Antibacterial Mode-of-Action Studies

2011 ◽  
Vol 55 (4) ◽  
pp. 1784-1786 ◽  
Author(s):  
Katherine R. Mariner ◽  
Nicola Ooi ◽  
Deborah Roebuck ◽  
Alex J. O'Neill ◽  
Ian Chopra

ABSTRACTWe further examined the usefulness of previously reportedBacillus subtilisbiosensors for antibacterial mode-of-action studies. The biosensors could not detect the tRNA synthetase inhibitors mupirocin, indolmycin, and borrelidin, some inhibitors of peptidoglycan synthesis, and most membrane-damaging agents. However, the biosensors confirmed the modes of action of several RNA polymerase inhibitors and DNA intercalators and provided new insights into the possible modes of action of ciprofloxacin, anhydrotetracycline, corralopyronin, 8-hydroxyquinoline, and juglone.

2013 ◽  
Vol 57 (4) ◽  
pp. 1948-1951 ◽  
Author(s):  
Yukinori Tanaka ◽  
Hideaki Nanamiya ◽  
Koichi Yano ◽  
Koji Kakugawa ◽  
Fujio Kawamura ◽  
...  

ABSTRACTBacillus subtiliscontains 10 rRNA (rrn) operons. We found that rRNA operon-engineeredB. subtilisstrain RIK543, with only therrnOoperon, is specifically hypersensitive to RNA polymerase inhibitors such as rifamycin SV and rifampin (80-fold and 20-fold, respectively). In pilot screening experiments, we found actinomycete isolates successfully at an incidence of 1.9% (18/945) that produced antibacterials that were detectable only with RIK543 as the test organism. Strain RIK543 may be a feasible test organism for the discovery of novel RNA polymerase inhibitors.


Planta Medica ◽  
2007 ◽  
Vol 73 (09) ◽  
Author(s):  
L Moujir ◽  
L de León ◽  
IL Bazzocchi

2020 ◽  
Vol 11 (1) ◽  
Author(s):  
Hao-Hong Pei ◽  
Tarek Hilal ◽  
Zhuo A. Chen ◽  
Yong-Heng Huang ◽  
Yuan Gao ◽  
...  

AbstractCellular RNA polymerases (RNAPs) can become trapped on DNA or RNA, threatening genome stability and limiting free enzyme pools, but how RNAP recycling into active states is achieved remains elusive. In Bacillus subtilis, the RNAP δ subunit and NTPase HelD have been implicated in RNAP recycling. We structurally analyzed Bacillus subtilis RNAP-δ-HelD complexes. HelD has two long arms: a Gre cleavage factor-like coiled-coil inserts deep into the RNAP secondary channel, dismantling the active site and displacing RNA, while a unique helical protrusion inserts into the main channel, prying the β and β′ subunits apart and, aided by δ, dislodging DNA. RNAP is recycled when, after releasing trapped nucleic acids, HelD dissociates from the enzyme in an ATP-dependent manner. HelD abundance during slow growth and a dimeric (RNAP-δ-HelD)2 structure that resembles hibernating eukaryotic RNAP I suggest that HelD might also modulate active enzyme pools in response to cellular cues.


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