The distal-proximal relationships among the human moonlighting proteins: Evolutionary hotspots and Darwinian checkpoints

Moonlighting proteins, known for their ability to perform multiple, often unrelated functions within a single polypeptide chain, challenge the traditional “one gene, one protein, one function” paradigm. As organisms evolved, their genomes remained relatively stable in size, but the introduction of p...

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Published in:International journal of biological macromolecules 2024-02, Vol.259 (Pt 1), p.128998-128998, Article 128998
Main Authors: Nawn, Debaleena, Hassan, Sk. Sarif, Sil, Moumita, Ghosh, Ankita, Goswami, Arunava, Basu, Pallab, Dayhoff, Guy W., Lundstrom, Kenneth, Uversky, Vladimir N.
Format: Article
Language:English
Subjects:
Distal-proximal
Moonlighting proteins
Phylogeny
Promiscuous proteins
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Summary:Moonlighting proteins, known for their ability to perform multiple, often unrelated functions within a single polypeptide chain, challenge the traditional “one gene, one protein, one function” paradigm. As organisms evolved, their genomes remained relatively stable in size, but the introduction of post-translational modifications and sub-strategies like protein promiscuity and intrinsic disorder enabled multifunctionality. Enzymes, in particular, exemplify this phenomenon, engaging in unrelated processes alongside their primary catalytic roles. This study employs a systematic, quantitative informatics approach to shed light on human moonlighting protein sequences. Phylogenetic analyses of human moonlighting proteins are presented, elucidating the distal-proximal relationships among these proteins based on sequence-derived quantitative features. The findings unveil the captivating world of human moonlighting proteins, urging further investigations in the emerging field of moonlighting proteomics, with the potential for significant contributions to our understanding of multifunctional proteins and their roles in diverse cellular processes and diseases.
ISSN:0141-8130
1879-0003
DOI:10.1016/j.ijbiomac.2023.128998