چکیده (انگلیسی):

Previous mass spectrometry analyses described human mitochondrial peptides entirely translated fromswinger
RNAs, RNAswhere polymerization systematically exchanged nucleotides. Exchanges follow one among 23 bijective
transformation rules, nine symmetric exchanges (X ↔ Y, e.g. A ↔ C) and fourteen asymmetric exchanges
(X → Y → Z → X, e.g. A → C → G → A), multiplying by 24 DNA's protein coding potential. Abrupt switches from
regular to swinger polymerization produce chimeric RNAs. Here, human mitochondrial proteomic analyses
assuming abrupt switches between regular and swinger transcriptions, detect chimeric peptides, encoded by
part regular, part swinger RNA. Contiguous regular- and swinger-encoded residues within single peptides are
stronger evidence for translation of swinger RNA than previously detected, entirely swinger-encoded peptides:
regular parts are positive controls matched with contiguous swinger parts, increasing confidence in results.
Chimeric peptides are 200× rarer than swinger peptides (3/100,000 versus 6/1000). Among 186 peptides
with N8 residues for each regular and swinger parts, regular parts of eleven chimeric peptides correspond to
six among the thirteen recognized, mitochondrial protein-coding genes. Chimeric peptides matching partly
regular proteins are rarer and less expressed than chimeric peptides matching non-coding sequences, suggesting
targeted degradation of misfolded proteins. Present results strengthen hypotheses that the short mitogenome
encodes far more proteins than hitherto assumed. Entirely swinger-encoded proteins could exist.