In contrast to human-made systems such as dedicated pieces of electronic hardware that have a single function in a single location (e.g., a temperature sensor), the divinely made proteins in cells are able to perform completely separate functions in different places. However, even this simple comparison isn’t really fair because individual human-made devices like sensor units still consist of multiple electronic components while a single cellular protein (that can also act like a sensor) is primarily a single defined and folded chain of amino acids. These amazing bioengineering marvels have been called moonlighting proteins, and they are utterly befuddling the evolutionary paradigm and its proponents.
Moonlighting proteins reside across the spectrum of life from single-cell bacteria to plants and animals, as well as humans.1,2 They are defined as “polypeptides [polymers of amino acids] that can perform two or more molecular functions within a single primary sequence.”2 While many genes in plant and animal genomes can produce a wide variety of protein variants due to their incredible functionality and density of encoded information,3 moonlighting proteins do not fit in this category but are actually the same protein sequence doing different tasks, often in completely separate locations.
Many moonlighting proteins are known to achieve this multifunctionality by being folded into different configurations that change their 3-D shape and thus their functional specificity.1 In addition to different functions, these proteins often perform different roles in completely different cellular compartments. In fact, some can even be found on the surface of the cell embedded in the membrane or even outside the cell in the extracellular matrix.
Evolutionists have great difficulty explaining the origin of any gene, much less those that produce moonlighting proteins. In the standard evolutionary paradigm, it is believed that so-called neutral mutations in pre-existing genes may be co-opted at some point to produce new functions. However, as noted in a recent secular journal paper that attempted to explain the evolutionary origin of moonlighting proteins, “this scenario is seemingly in conflict with the fact that mutations in the coding sequences of genes tend to be deleterious.”2 The study’s authors go on to fancifully claim these genes arose by being duplicated from other genes and then going through some magical process of rapid alteration. However, the whole idea of gene duplication being able to explain gene origins and function is now being actively refuted by empirical data produced by evolutionists themselves.4 Ultimately, the authors concluded their paper by stating, “The evolutionary pathways leading to the generation, retention, and loss of moonlighting proteins remain largely unknown.”2
Perhaps the most damaging evidence for the whole evolutionary paradigm regarding moonlighting proteins is the fact that in humans, their dysfunction is associated with disease.1 Whether the same moonlighting protein is functioning in the nucleus to regulate gene expression or embedded in the cell membrane functioning as an elaborate sensor-receptor, its mission-critical activities are precisely regulated.5 In other words, there is no wiggle room for any random “evolutionary tinkering.”
The precise multifunctional biocomplexity of these proteins—all encoded in the same sequence—is direct and powerful evidence of an omnipotent Creator’s handiwork, not purposeless evolution based on chance.
- Jeffery, C. J. 2015. Why study moonlighting proteins? Frontiers in Genetics. 6: 211.
- Espinosa-Cantú, A. et al. 2015. Gene duplication and the evolution of moonlighting proteins. Frontiers in Genetics. 6: 227.
- Tomkins, J. 2015. Extreme Information: Biocomplexity of Interlocking Genome Languages. Creation Research Society Quarterly. 51 (3): 187-201.
- Hargreaves, A. D. et al. 2014. Restriction and recruitment – gene duplication and the origin and evolution of snake venom toxins. Genome Biology and Evolution. 6 (8): 2088-2095.
- Boshnjaku, V. et al. 2012. Nuclear localization of folate receptor alpha: a new role as a transcription factor. Scientific Reports. 2: 980.5.
* Dr. Tomkins is Research Associate at the Institute for Creation Research and received his Ph.D. in genetics from Clemson University.
Cite this article: Jeffrey P. Tomkins, Ph.D. 2015. Moonlighting Proteins Befuddle Evolution. Acts & Facts. 44 (9).