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Published on: January 13, 2016
Coding palindromes in mitochondrial genes of Nematomorpha
Kirill V Mikhailov1,2, Boris D Efeykin2,3, Alexander Y Panchin2
1Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Leninskiye Gory 1-40, Moscow 119991, Russian Federation.
Mitochondrial DNA in Nematomorpha contains long inverted repeats within protein-coding genes. These genes encode functional proteins, revealing a unique evolutionary strategy balancing DNA structure and protein function.
Area of Science:
- Genomics
- Molecular Biology
- Evolutionary Biology
Background:
- Inverted repeats are DNA sequences that can form secondary structures.
- These structures typically avoid protein-coding regions due to potential conflicts with protein function.
Purpose of the Study:
- To investigate the presence and implications of inverted repeats within protein-coding genes.
- To understand the evolutionary mechanisms allowing simultaneous preservation of DNA structure and protein function.
Main Methods:
- Bioinformatic analysis of mitochondrial genomes from four Nematomorpha species.
- Sequence analysis to identify and characterize inverted repeats.
- Confirmation of gene transcription and protein function (respiratory complex I).
Main Results:
- Discovery of numerous long perfect inverted repeats (up to 284 bp) within mitochondrial protein-coding genes of Nematomorpha.
- Both arms of these repeats encode conserved amino acid sequences.
- Genes containing inverted repeats are transcribed and translated into functional proteins, evidenced by respiratory complex I activity.
- Evidence of strong selection at the amino acid level in these regions.
- Similar, though shorter, embedded repeats found in other organisms' mitochondrial genomes.
Conclusions:
- Nematomorpha mitochondrial genomes exhibit an unusual evolutionary compromise, maintaining functional protein coding despite embedded inverted repeats.
- These findings challenge the general assumption that inverted repeats are excluded from coding sequences.
- The study highlights a novel mechanism for preserving both secondary DNA structure and essential protein function.
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