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- For the last six decades, cytochrome P450 monooxygenases (CYPs/P450s), heme thiolate proteins, have been under the spotlight due to their regio- and stereo-selective oxidation activities, which has led to the exploration of their applications in almost all known areas of biology. The availability of many genome sequences allows us to understand the evolution of P450s in different organisms, especially in the Bacteria domain. The phenomenon that “P450s play a key role in organisms’ adaptation vis a vis lifestyle of organisms impacts P450 content in their genome” was proposed based on studies on a handful of individual bacterial groups. To have conclusive evidence, one must analyze P450s and their role in secondary metabolism in species with diverse lifestyles but that belong to the same category. We selected species of the phylum Proteobacteria classes, Alpha, Beta, Gamma, Delta, and Epsilon, to address this research gap due to their diverse lifestyle and ancient nature. The study identified that the lifestyle of alpha-, beta-, gamma-, delta-, and epsilon-proteobacterial species profoundly affected P450 profiles in their genomes. The study determined that irrespective of the species associated with different proteobacterial classes, pathogenic species or species adapted to a simple lifestyle lost or had few P450s in their genomes. On the contrary, species with saprophytic or complex lifestyles had many P450s and secondary metabolite biosynthetic gene clusters. The study findings prove that the phenomenon mentioned above is factual, and there is no link between the number and diversity of P450s and the age of the bacteria.
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- Proline-, Glutamic acid-, Leucine-rich Protein 1 (PELP1) is a multifunctional nuclear protein essential for ribosome biogenesis and steroid receptor signaling. It contains two hallmark domains: the RIX1 (Ribosome Export 1) domain, which mediates rRNA processing, and the NUC (nucleolar) domain, associated with nucleolar function. While PELP1’s biological roles are well-characterized in mammals, particularly Homo sapiens, its distribution, structural diversity, and evolutionary origin across the domain of life remain largely unexplored. This study addresses this gap by conducting a comprehensive data mining of PELP1 proteins across the NCBI, UniProt, and EukProt databases. A total of 646 PELP1 proteins were identified exclusively in eukaryotes, specifically within the Opisthokonta clade, comprising Fungi, Filasterea, and Metazoa, while no homologs were detected in Bacteria, Viruses, Plants, or Oomycota. Domain analysis revealed that PELP1 proteins contain one RIX1 domain and one or two NUC202 domains. Motif analysis identified LXXLL and PXXP motifs, indicative of receptor-mediated signaling capability, although leucine and proline residues were not universally conserved within these motifs. Amino acid composition analysis showed enrichment of proline, glutamic acid, and cysteine across most PELP1 proteins. Despite low overall sequence identity, structural modeling demonstrated strong conservation of the α-helical fold, with an average root-mean-square deviation (RMSD) of 1.9 Å across species. Evolutionary analysis suggests that ancestral PELP1 emerged before the divergence of opisthokonts, originating from an RIX1-domain-containing protein that subsequently acquired a NUC202 domain. Phylogenetic clustering and sequence identity patterns resolved three major evolutionary lineages corresponding to fungi, filastereans, and metazoans. Overall, these findings reveal that PELP1 proteins exhibit extensive sequence divergence while maintaining a conserved structural architecture, reflecting evolutionary adaptation that preserves functional integrity across opisthokonts.
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