in silico analysis and molecular modeling of rna polymerase, sigma s (rpos) protein in pseudomonas aeruginosa pao1

Authors

mansour sedighi department of microbiology, faculty of medicine, iran university of medical sciences, tehran, iran

mohsen moghoofei department of virology, faculty of medicine, iran university of medical sciences, tehran, iran

ebrahim kouhsari department of microbiology, faculty of medicine, iran university of medical sciences, tehran, iran

abazar pournajaf department of microbiology, faculty of medicine, iran university of medical sciences, tehran, iran

abstract

background: sigma factors are proteins that regulate transcription in bacteria. sigma factors can be activated in response to different environmental conditions. the rpos (rna polymerase, sigma s) gene encodes sigma-38 (σ38, or rpos), a 37.8 kda protein in pseudomonas aeruginosa (p. aeruginosa) strains. rpos is a central regulator of the general stress response and operates in both retroactive and proactive manners; not only does it allow the cell to survive environmental challenges; it also prepares the cell for subsequent stresses (cross-protection). methods: the significance of rpos for stress resistance and protein expression in stationary-phase p. aeruginosa cells was assessed. the goal of the current study was to characterize rpos of p. aeruginosa pao1 using bioinformatics tools. results: the results showed that rpos is an unstable protein that belongs to the sigma-70 factor family. secondary structure analysis predicted that random coil is the predominant structure followed by extended alpha helix. the three-dimensional (3d) structure was modeled using swiss-model workspace. conclusion: determination of sequence, function, structure, and predicted epitopes of rpos is important for modeling of inhibitors that will help in the design of new drugs to combat multi-drug-resistant (mdr) strains. such information may aid in the development of new diagnostic tools, drugs, and vaccines for treatment in endemic regions.

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Journal title:
reports of biochemistry and molecular biology

جلد ۴، شماره ۱، صفحات ۳۲-۴۲

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