Caenorhabditis elegans triple null mutant lacking UDP-N-acetyl-D-glucosamine:alpha-3-D-mannoside beta1,2-N-acetylglucosaminyltransferase I.
Caenorhabditis elegans triple null mutant lacking UDP-N-acetyl-D-glucosamine:alpha-3-D-mannoside beta1,2-N-acetylglucosaminyltransferase I.
复制标题
秀丽隐杆线虫三无效突变体缺乏 UDP-N-乙酰基-D-葡萄糖胺:α-3-D-甘露糖苷 beta1,2-N-乙酰基葡萄糖胺基转移酶 I。
DOI:
10.1042/bj20040793
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发表时间:
2004
期刊:
影响因子:
--
通讯作者:
Schachter,Harry
中科院分区:
文献类型:
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作者:
Zhu,Shaoxian;Hanneman,Andrew;Reinhold,VernonN;Spence,AndrewM;Schachter,Harry
We have previously reported, from the nematode wormCaenor-habditis elegans, three genes (gly-12,gly-13andgly-14) encoding enzymically active UDP-N-acetyl-D-glucosamine:α-3-D-mannoside β1,2-N-acetylglucosaminyltransferase I (GnT I), an enzyme essential for hybrid, paucimannose and complexN-glycan synthesis. We now describe a worm with null mutations in all three GnT I genes,gly-14 (III);gly-12 gly-13 (X)(IIIandXrefer to the chromosome number). The triple-knock-out (TKO) worms have a normal phenotype, although they do not express GnT I activity and do not synthesize 31 paucimannose, complex and fucosylated oligomannoseN-glycans present in the wild-type worm. The TKO worm has increased amounts of non-fucosylated oligomannoseN-glycan structures, a finding consistent with the site of GnT I action. Five fucosylated oligomannoseN-glycan structures were observed in TKO, but not wild-type, worms, indicating the presence of unusual GnT I-independent fucosyltransferases. It is concluded that wild-typeC. elegansmakes a large number of GnT I-dependentN-glycans that are not essential for normal worm development under laboratory conditions. The TKO worm may be more susceptible to mutations in other genes, thereby providing an approach for the identification of genes that interact with GnT I.