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Pms2 suppresses large expansions of the (GAA·TTC)n sequence in neuronal tissues.
- Source :
-
PloS one [PLoS One] 2012; Vol. 7 (10), pp. e47085. Date of Electronic Publication: 2012 Oct 11. - Publication Year :
- 2012
-
Abstract
- Expanded trinucleotide repeat sequences are the cause of several inherited neurodegenerative diseases. Disease pathogenesis is correlated with several features of somatic instability of these sequences, including further large expansions in postmitotic tissues. The presence of somatic expansions in postmitotic tissues is consistent with DNA repair being a major determinant of somatic instability. Indeed, proteins in the mismatch repair (MMR) pathway are required for instability of the expanded (CAG·CTG)(n) sequence, likely via recognition of intrastrand hairpins by MutSβ. It is not clear if or how MMR would affect instability of disease-causing expanded trinucleotide repeat sequences that adopt secondary structures other than hairpins, such as the triplex/R-loop forming (GAA·TTC)(n) sequence that causes Friedreich ataxia. We analyzed somatic instability in transgenic mice that carry an expanded (GAA·TTC)(n) sequence in the context of the human FXN locus and lack the individual MMR proteins Msh2, Msh6 or Pms2. The absence of Msh2 or Msh6 resulted in a dramatic reduction in somatic mutations, indicating that mammalian MMR promotes instability of the (GAA·TTC)(n) sequence via MutSα. The absence of Pms2 resulted in increased accumulation of large expansions in the nervous system (cerebellum, cerebrum, and dorsal root ganglia) but not in non-neuronal tissues (heart and kidney), without affecting the prevalence of contractions. Pms2 suppressed large expansions specifically in tissues showing MutSα-dependent somatic instability, suggesting that they may act on the same lesion or structure associated with the expanded (GAA·TTC)(n) sequence. We conclude that Pms2 specifically suppresses large expansions of a pathogenic trinucleotide repeat sequence in neuronal tissues, possibly acting independently of the canonical MMR pathway.
- Subjects :
- Adenosine Triphosphatases genetics
Animals
Cerebellum metabolism
DNA Mismatch Repair
DNA Repair Enzymes genetics
DNA-Binding Proteins genetics
Friedreich Ataxia genetics
Ganglia, Spinal metabolism
Genomic Instability
Humans
Mice
Mice, Transgenic
Mismatch Repair Endonuclease PMS2
MutS DNA Mismatch-Binding Protein genetics
MutS DNA Mismatch-Binding Protein metabolism
MutS Homolog 2 Protein genetics
MutS Homolog 2 Protein metabolism
Mutation
Adenosine Triphosphatases metabolism
DNA Repair Enzymes metabolism
DNA-Binding Proteins metabolism
Trinucleotide Repeat Expansion
Subjects
Details
- Language :
- English
- ISSN :
- 1932-6203
- Volume :
- 7
- Issue :
- 10
- Database :
- MEDLINE
- Journal :
- PloS one
- Publication Type :
- Academic Journal
- Accession number :
- 23071719
- Full Text :
- https://doi.org/10.1371/journal.pone.0047085