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 language | English (US) |
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Pages (from-to) | 1657-1661 |
Number of pages | 5 |
Journal | Human molecular genetics |
Volume | 5 |
Issue number | 10 |
DOIs | |
State | Published - Oct 1996 |
Funding
This work was supported by NIH grant HD48258 to B.W. We thank Karen Norrgard, Kristin Fleischhauer, Jeanne Hymes, and Greg Meyers for technical assistance and advice, and Dr Marilyn Cowger and Cheryl Clow, RN, at the Children’s Hospital at Albany Medical Center for providing samples and medical history from this patient and his family.
ASJC Scopus subject areas
- Genetics(clinical)
- Genetics
- Molecular Biology