Structure of the human biotinidase gene

Mammalian Genome

Volumn 9, Issue 4, 1998, Pages 327-330

  Knight, Heath Cole ^a,c   Reynolds, Thomas R ^b   Meyers, Gregory A ^b   Pomponio, Robert J ^a,d   Buck, Gregory A ^a,b   Wolf, Barry ^a  

^a VIRGINIA COMMONWEALTH UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b Commonwealth Biotechnologies Inc ^*  (United States)

^c MAYO CLINIC   (United States)

^d GENZYME CORPORATION   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

GENE SEQUENCING; HUMAN GENE; HUMAN GENOME;

AMIDOHYDROLASES; BASE SEQUENCE; BIOTINIDASE; DNA, COMPLEMENTARY; EXONS; HUMANS; INTRONS; MOLECULAR SEQUENCE DATA; POLYMERASE CHAIN REACTION;

EID: 0032054470     PISSN: 09388990     EISSN: None     Source Type: Journal    
DOI: 10.1007/s003359900760     Document Type: Article

References (23)

1. Achuta Murthy PN, Mistry SP (1977) Biotin Prog Food Nutr Sci 2, 405-455
2. Bird AP (1986) CpG-rich islands and the function of DNA methylation. Nature 321, 209-213
3. Cole H (1994) Cloning and characterization of the human biotinidase gene (Richmond, Va.: Doctoral Thesis, Medical College of Virginia/Virginia Commonwealth University)
4. Cole H, Reynolds TR, Buck GB, Lockyer JM, Denson T, Spence JE, Hymes J, Wolf B (1994a) Human serum biotinidase: cDNA cloning, sequence and characterization. J Biol Chem 269, 6566-6570
5. Cole H, Weremowicz H, Morton CC, Wolf B (1994b) Localization of serum biotinidase (BTD) to human chromosome 3 in band p25. Genomics 22, 662-663
6. Grange T, Roux J, Rigaud G, Pictet R (1990) Cell-type specific activity of two glucocorticoid responsive units of rat tyrosine aminotransferase gene is associated with multiple binding sites for C/EBP and a novel liver-specific nuclear factor. Nucleic Acids Res 19, 131-139
7. Hecker KH, Roux KH (1996) High and low annealing temperatures increase both specificity and yield in touchdown and stepdown PCR. BioTech 20, 478-484
8. Jackson IJ (1991) A reappraisal of non-consensus mRNA splice sites. Nucleic Acids Res 19, 3795-3798
9. Jacob M, Gallinaro H (1989) The 5′-splice site: phylogenetic evolution and variable geometry of the association with UIRNA. Nucleic Acids Res 17, 2159-2180
10. Lewin B (1997) Genes VI (Oxford: Oxford University Press)
11. Norrgard KJ, Pomponio RJ, Swango KL, Hymes J, Reynolds TR, Buck GA, Wolf B (1997a) Double mutation (A171T and D444H) is a common cause of profound biotinidase deficiency in children ascertained by newborn screening in United States. Hum Mutat
12. Norrgard KJ, Pomponio RJ, Swango KL, Hymes J, Reynolds TR, Buck GA, Wolf B (1997b) Mutation (Q456H) is the most common cause of profound biotinidase deficiency in children ascertained by newborn screening in the United States. Biochem Mol Med 61, 22-27
13. Perlman D, Halvorson HO (1983) A putative signal recognition site and sequence in eukaryotic and prokaryotic signal peptides. J Mol Biol 167, 391-409
14. Pispa J (1965) Animal biotinidase. Ann Med Exp Biol Fenn 43 (Suppl 5), 1-39
15. Pomponio RJ, Reynolds TR, Cole H, Buck GA, Wolf B (1995) Mutational "hotspot" in the human biotinidase gene as a cause of biotinidase deficiency. Nat Genet 11, 96-98
16. Pomponio RJ, Narasimhan V, Reynolds TR, Buck GA, Povirk LF. Wolf B (1996) Deletion/insertion mutation that causes biotinidase deficiency may result from the formation of a quasipalindromic structure. Hum Mol Genet 5, 1657-1661
17. Pomponio RJ, Norrgard KJ, Reynolds TR, Hymes J, Buck GA, Wolf B (1997a) Arg538 to Cys mutation in a CpG dinucleotide of the human biotinidase gene is the second most common cause of biotinidase deficiency in symptomatic children with biotinidase deficiency. Hum Genet 99, 506-512
18. Pomponio RJ, Reynolds TR, Mandel H, Admoni O, Melone PD, Buck GA, Wolf B (1997b) Profound biotinidase deficiency caused by a point mutation that creates a downstream cryptic 3′ splice acceptor site within an exon of the human biotinidase gene. Hum Mol Genet 6, 739-745
19. Sambrook J, Fritsch EF, Maniatis T (1989) Analysis and cloning of eukaryotic genomic DNA. In Molecular Cloning: A Laboratory Manual. (Cold Spring Harbor, N.Y.: Cold Spring Harbor Laboratory Press), pp 9.44-9.5
20. Smale ST, Baltimore D (1989) The "initiator" as a transcription control element. Cell 57, 103-113
21. Wolf B (1995) Disorders of hiotin metabolism. In The Metabolic and Molecular Bases of Inherited Disease, CR Scriver, AL Beaudet, WS Sly, D Valle, eds. (New York: McGraw-Hill, Inc.), pp 3151-3180
22. Wolf B, Feldman GL (1982) The biotin-dependent carboxylase deficiencies. Am J Hum Genet 34, 699-716
23. Wolf B, Grier RE, Allen RJ, Goodman SI, Kien CL (1983). Biotinidase deficiency: the enzymatic defect in late-onset multiple carboxylase deficiency. Clin Chim Acta 131, 273-281