Abstract |
Mutations in the E3-binding protein component of pyruvate dehydrogenase complex have been demonstrated in a few cases of Leigh syndrome. We report that two mutations previously detected in the E3-binding protein cDNA are the consequence of splice-site mutations. Both involved a single base substitution in the conserved dinucleotides of splice junctions, one leading to skipping of an exon and the other, to activation of a cryptic site. Our findings add to the understanding of molecular basis of E3-binding protein deficiency and indicate yet again the high frequency of splicing mutations in this gene.
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Authors | Runu Dey, Bernard Aral, Marc Abitbol, Cecile Marsac |
Journal | Molecular genetics and metabolism
(Mol Genet Metab)
Vol. 76
Issue 4
Pg. 344-7
(Aug 2002)
ISSN: 1096-7192 [Print] United States |
PMID | 12208141
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
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Chemical References |
- PDHX protein, human
- Peptides
- Pyruvate Dehydrogenase Complex
- RNA Splice Sites
- Lactic Acid
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Topics |
- Amino Acid Sequence
- Base Sequence
- Humans
- Lactic Acid
(blood)
- Leigh Disease
(etiology, genetics, metabolism)
- Molecular Sequence Data
- Mutation
- Peptides
(genetics)
- Pyruvate Dehydrogenase Complex
(genetics)
- RNA Splice Sites
(genetics)
- Sequence Deletion
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