Characterization of Fut10 and Fut11, Putative Alpha-1-3/4 Fucosyltransferase Genes Important for Vertebrate Development
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- Department of Cell Biology, Albert Einstein College of Medicine, New York, USA
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- Manuscript
- Date:
- Received 20 June 2007 20:53 UTC; Posted 20 June 2007
- Subjects:
- Developmental Biology, Molecular Cell Biology
- Abstract:
Two new, putative alpha-1-3/4 fucosyltransferases (α1-3/4 Fuc-Ts), Fuc-TX and Fuc-TXI, were identified in the vertebrate genome and transcriptome sequence databases through sequence homology-based queries. These proteins have a significant sequence similarity to only α1-3/4 Fuc-Ts, and possess peptide motifs that are evolutionarily conserved among the known vertebrate α1-3/4 Fuc-Ts. However, Fuc-TX and Fuc-TXI lack the HH[R/W][D/E] sequence that determines the specificity for type 1 or 2 substrates among the known vertebrate enzymes, and Fuc-TXI proteins do not possess a transmembrane domain. The Fut10 and Fut11 genes that encode these proteins are expressed ubiquitously in the adult mouse and in the mouse embryo throughout development. Though a Fuc-T activity of the mouse proteins could not be detected, Fuc-TXI, but not Fuc-TX, was found to hydrolyze GDP-fucose. The interaction of Fuc-TXI with GDP-fucose was also confirmed by its binding to GDP-hexanolamine. In zebrafish, Fut11 transcripts could be detected during early embryonic development. A knock-down of Fuc-TXI in zebrafish embryos with Fut11-specific antisense morpholino oligonucleotides resulted in malformations of the posterior trunk and tail.
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Patnaik, Santosh. Characterization of Fut10 and Fut11, Putative Alpha-1-3/4 Fucosyltransferase Genes Important for Vertebrate Development. Available from Nature Precedings <http://hdl.handle.net/10101/npre.2007.141.1> (2007)
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Santosh Patnaik on 01 January 2009 02:59 UTC
Mollicone, et al., have finally demonstrated the α1,3-fucosyltransferase activity of Fut10 and Fut11 (fucose transferred to the chitobiose core of N-glycans). The work is published in the Journal of Biological Chemistry.