Evolutionary aspects of the Viridiplantae nitroreductases

Abstract

Background Nitroreductases are a family of evolutionarily related proteins catalyzing the reduction of nitro-substituted compounds. Nitroreductases are widespread enzymes, but nearly all modern research and practical application have been concentrated on the bacterial proteins, mainly nitroreductases of Escherichia coli. The main aim of this study is to describe the phylogenic distribution of the nitroreductases in the photosynthetic eukaryotes (Viridiplantae) to highlight their structural similarity and areas for future research and application. Results This study suggests that homologs of nitroreductase proteins are widely presented also in Viridiplantae. Maximum likelihood phylogenetic tree reconstruction method and comparison of the structural models suggest close evolutional relation between cyanobacterial and Viridiplantae nitroreductases. Conclusions This study provides the first attempt to understand the evolution of nitroreductase protein family in Viridiplantae. Our phylogeny estimation and preservation of the chloroplasts/mitochondrial localization indicate the evolutional origin of the plant nitroreductases from the cyanobacterial endosymbiont. A defined high level of the similarity on the structural level suggests conservancy also for the functions. Directions for the future research and industrial application of the Viridiplantae nitroreductases are discussed.

Cd-induced cytosolic proteome changes in the cyanobacterium Anabaena sp. PCC7120 are mediated by LexA as one of the regulatory proteins

“…Among the 10 identified hypothetical proteins, Alr0803, which exhibited similarity with signal transduction histidine kinase, was earlier suggested not to be regulated by LexA based on in silico and transcript analyses, and Alr0882, which showed similarity with universal stress protein domain-containing proteins, was earlier predicted to be regulated by LexA due to the presence of AnLexA-Box near to the -10 region (Table 2, Srivastava et al, 2022b PREPRINT). All1864 shared similarities with nitroreductases, which have been implicated in response to oxidative stress (Dabravolski, 2020). All1864 accumulation was unaffected by LexA overexpression under unstressed conditions but elevated by Cd stress at both the mRNA and protein levels in both recombinant Anabaena strains (Fig.…”

Cd-induced cytosolic proteome changes in the cyanobacterium Anabaena sp. PCC7120 are mediated by LexA as one of the regulatory proteins

“…Among the 10 identified hypothetical proteins, Alr0803, which exhibited similarity with signal transduction histidine kinase, was earlier suggested not to be regulated by LexA based on in silico and transcript analyses, and Alr0882, which showed similarity with universal stress protein domain-containing proteins, was earlier predicted to be regulated by LexA due to the presence of AnLexA-Box near to the −10 region (Table 2, Srivastava et al, 2022b PREPRINT). All1864 shared similarities with nitroreductases, which have been implicated in response to oxidative stress (Dabravolski, 2020). All1864 accumulation was unaffected by LexA overexpression under unstressed conditions but elevated by Cd stress at both the mRNA and protein levels in both recombinant Anabaena strains (Fig.…”

Microbial nitroreductases: A versatile tool for biomedical and environmental applications

“…FMN or FAD is possessed by them, as a prosthetic group [11,19]. A lot of these NRs are found mostly in bacterial species and also found in archaea and eukaryotes [20] to a little extent. Knowledge of the biochemical functions of NRs is very limited.…”