Deletion/insertion mutation that causes biotinidase deficiency may result from the formation of a quasipalindromic structure

Robert J. Pomponio, Vasant Narasimhan, Thomas R. Reynolds, Gregory A. Buck, Lawrence F. Povirk, Barry Wolf*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

17 Scopus citations

Abstract

Biotinidase is responsible for recycling the vitamin biotin from biocytin that is formed after the proteolytic degradation of the biotin-dependent carboxylases. We have identified a deletion/insertion mutation within exon D of the human biotinidase gene in a child with biotinidase deficiency. The mutation causes a frame shift and premature termination which are predicted to result in a truncated protein. We propose that the mutation occurred during DNA replication by either of two mechanisms. Both mechanisms involve formation of a quasipalindromic hairpin loop in the template and dissociation of DNA polymerase α. This mutation supports the formation of palindromic structures as a possible cause of deletions in eukaryotes, and supports the proposal, derived from in vitro studies, that polymerase α may preferentially arrest or dissociate at specific template sequences.

Original languageEnglish (US)
Pages (from-to)1657-1661
Number of pages5
JournalHuman molecular genetics
Volume5
Issue number10
DOIs
StatePublished - Oct 1996

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics
  • Genetics(clinical)

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