Natural mitochondrial proteolysis confirms transcription systematically exchanging/deleting nucleotides, peptides coded by expanded codons. (7th February 2017)

• Record Type: Journal Article
• Authors: Seligmann, Hervé
• Is Part Of: Journal of theoretical biology. Volume 414(2017)
• Page Start: 76
• Page End: 90
• Publication Date: 2017-02-07
• Subjects: Frameshifting transcription -- Translational frameshift -- Bijective transformation -- Digestive enzymes -- Proteome -- Systematic deletions -- DelRNA; Biology -- Periodicals; Biological Science Disciplines -- Periodicals; Biology -- Periodicals; Biologie -- Périodiques; Theoretische biologie; Biology; Periodicals; 571.05
• DOI: 10.1016/j.jtbi.2016.11.021
• Languages: English
• ISSNs: 0022-5193

Abstract

Abstract: Protein sequences have higher linguistic complexities than human languages. This indicates undeciphered multilayered, overprinted information/genetic codes. Some superimposed genetic information is revealed by detections of transcripts systematically (a) exchanging nucleotides (nine symmetric, e.g. A<->C, fourteen asymmetric, e.g. A->C->G->A, swinger RNAs) translated according to tri-, tetra- and pentacodons, and (b) deleting mono-, dinucleotides after each trinucleotide (delRNAs). Here analyses of two independent proteomic datasets considering natural proteolysis confirm independently translation of these non-canonical RNAs, also along tetra- and pentacodons, increasing coverage of putative, cryptically encoded proteins. Analyses assuming endoproteinase GluC and elastase digestions (cleavages after residues D, E, and A, L, I, V, respectively) detect additional peptides colocalizing with detected non-canonical RNAs. Analyses detect fewer peptides matching GluC-, elastase- than trypsin-digestions: artificial trypsin-digestion outweighs natural proteolysis. Results suggest occurrences of complete proteins entirely matching non-canonical, superimposed encoding(s). Protein-coding after bijective transformations could explain genetic code symmetries, such as along Rumer's transformation. Highlights: Trypsinized mitochondrial peptide data include elastase/GluC-digested peptides. These confirm non-canonical transcriptions/translations, map on non-canonical RNAs. Hence elastase- and GluC-like proteolysis occurs in human mitochondria. Alternative proteolyses confirm/expand analyses assuming trypsin-digestion. Multiple detections of a peptide means higher frequency, not detection quality.