Abstract
As an ATP-dependent protease, the quality control functions of Lon have been extensively studied and reviewed in the literature. By contrast, very little research has been conducted to investigate Lon’s physiological functions and its mechanism as a regulatory protease. In this manuscript, we provided a survey of literature and data to convey that the lambda N (λN) protein is a suitable Escherichia coli Lon (ELon) substrate for studying the role played by Lon in regulating an RNA transcription process. For proof of principle, we demonstrated that the minimal component of the RNA transcription complex containing RNA polymerase (RNAP) and the σ factor can inhibit λN degradation by ELon through SDS-PAGE, and the carboxyl-terminal of λN is important for Lon competing with RNAP interaction. Using negative stain electron microscopy, we obtained structural evidence to show that λN lacking the carboxyl-terminal flanked by residues 99-107 interacted with ELon differently than full-length λN. Taken together, the activity and EM data provide a starting point for performing a physiological enzymology study on the contribution of ELon toward RNA transcription.
Competing Interest Statement
The authors have declared no competing interest.
