Natural mitochondrial proteolysis confirms transcription systematically exchanging/deleting nucleotides, peptides...

Area of Science:

• Genomics
• Proteomics
• Bioinformatics

Background:

• Protein sequences exhibit linguistic complexity exceeding human languages, suggesting undiscovered genetic information.
• The existence of superimposed genetic codes, including swinger RNAs and delRNAs, has been proposed.

Purpose of the Study:

• To investigate the translation of non-canonical RNAs into proteins using proteomic data.
• To confirm the independent translation of these RNAs along various codon lengths (tri-, tetra-, pentacodons).
• To explore the implications of these findings for understanding genetic code symmetries.

Main Methods:

• Analysis of two independent proteomic datasets.
• Consideration of natural proteolysis, specifically endoproteinase GluC and elastase digestions.
• Detection and colocalization of peptides with non-canonical RNAs.
• Comparison of natural proteolysis with artificial trypsin digestion.

Main Results:

• Confirmation of independent translation of non-canonical RNAs, including swinger RNAs and delRNAs, into proteins.
• Detection of additional peptides that colocalize with non-canonical RNAs following specific enzyme digestions.
• Observation that artificial trypsin digestion yields more peptides than natural proteolysis (GluC, elastase).
• Evidence suggests complete proteins may be encoded by these superimposed, non-canonical genetic systems.

Conclusions:

• Non-canonical RNAs are translated into proteins, increasing the repertoire of potentially encoded proteins.
• Superimposed genetic codes and non-standard codon usage (tetra-, pentacodons) are biologically relevant.
• These findings offer a potential explanation for genetic code symmetries and bijective transformations.