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Pyruvate dehydrogenase deficiency as a result of splice-site mutations in the PDX1 gene.

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.
AuthorsRunu Dey, Bernard Aral, Marc Abitbol, Cecile Marsac
JournalMolecular genetics and metabolism (Mol Genet Metab) Vol. 76 Issue 4 Pg. 344-7 (Aug 2002) ISSN: 1096-7192 [Print] United States
PMID12208141 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
Chemical References
  • PDHX protein, human
  • Peptides
  • Pyruvate Dehydrogenase Complex
  • RNA Splice Sites
  • Lactic Acid
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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