{'fraction_non_alphanumeric': 0.02309782608695652, 'fraction_numerical': 0.0, 'mean_word_length': 5.012244897959183, 'pattern_counts': {'":': 0, '<': 0, '<?xml version=': 0, '>': 0, 'https://': 0, 'lorem ipsum': 0, 'www.': 0, 'xml': 0}, 'pii_count': 0, 'substrings_counts': 0, 'word_list_counts': {'cursed_substrings.json': 0, 'profanity_word_list.json': 0, 'sexual_word_list.json': 0, 'zh_pornsignals.json': 0}}
Inhibition of Lon protease by bacterial lipopolisaccharide (LPS) though inhibition of ATPase

Lon protease, an ATP-dependent protease in Escherichia coli, degrades 
abnormal proteins and regulates several important cellular functions. Here we 
show novel inhibitory effects of lipopolysaccharide (LPS) on Lon protease 
activities. LPS inhibited the peptidase, protease, and ATPase activities of 
Lon; and a dose-response study showed that LPS at low doses more effectively 
inhibited the ATPase activity than the peptidase one, suggesting different 
susceptibility to LPS of these activities associated with Lon. Structure-activity relationship studies revealed that 
ReLPS, detoxified LPS, and mono-phosphoryl as well as diphosphoryl 
lipid A, also showed similar inhibition, suggesting that neither O-antigen 
polysaccharide nor O-acyl chain, but rather phosphate groups in the lipid A 
domain, seem to have been responsible for the inhibitory effects. Besides, 
LPS was co-precipitated with Lon by an anti-Lon antibody, showing the direct 
binding of LPS to Lon. These results suggest that LPS bound to Lon and 
inhibited the protease activity of Lon by inhibiting its ATPase activity. These 
results also seem to be another example of a negatively charged phosphate 
group in membrane components of Escherichia coli being involved in the 
regulation of protease activity of Lon through binding to Lon and inhibiting 
its ATPase activity, as in the case of cardiolipin.