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Abstract
The reasons for the significant impact of abnormal tau protein phosphorylation and aggregation on Alzheimer's disease are still unknown. This study used bioinformatics methods, including protein domain search tools, to investigate the pathogenic mechanism of tau protein in neurodegenerative diseases. The study reveals that tau protein possesses domains linked to the Aging Device. These domains include pyruvate kinase, phosphatase, telomere binding, telomere transposition, HNH cas9, replicon binding, helicase, DNA polymerase, nuclease, transcription factors-like, promoter binding (TATA-box), enhancer binding (Homeobox, MADS-box, HMG box), and mitochondrial localization and mtDNA polymerase. It implies that the tau protein's pyruvate kinase domain supplies ATP energy for its Aging Device function. The HNH Cas9 , reverse transcriptase, and transposase domains cut the sequence between "TAA" from the telomere and then transcript the guide RNA sequence. The transcription factor domain slides to the specific DNA transcription factor binding region. The HNH Cas9 domain excises the intron DNA region complementary to the guide RAN sequence. The transposase and nuclease domains splice the "TAA" from the promoter or enhancer and add the telomere fragment sequence. We thought that tau protein transposes telomere fragments to the promoter/enhancer region might mess up RNA polymerase II, which would help the Aging Device's telomere-guided gene (DNA in the nucleus or mitochondrial) copy number decrement regulation system work better. It can help us understand how stress injuries, like low blood sugar or oxygen levels, can cause tau protein to clump together and phosphorylate, which turns off the Aging Device in a way that doesn't make sense. Thus, the anomalous work of aging devices, such as tau protein, may be associated with neurodegenerative diseases like Alzheimer disease, amyotrophic lateral sclerosis.
