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.
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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:
The Biochemical journal.
影响因子:
--
通讯作者:
Schachter,Harry
Schachter,Harry
中科院分区:
--
文献类型:
--
作者:
Zhu,Shaoxian;Hanneman,Andrew;Reinhold,VernonN;Spence,AndrewM;Schachter,Harry

文献摘要

相似文献

我们之前报道过,来自线虫秀丽隐杆线虫的三个基因(gly-12、gly-13和gly-14)编码具有酶活性的UDP-N-乙酰-D-葡萄糖胺:α-3-D-甘露糖苷β1,2-N-乙酰葡萄糖胺基转移酶I(GnT I),这是一种杂交所必需的酶, 少量甘露糖和复杂的N-聚糖合成。我们现在描述了一种在所有三个 GnT I 基因,gly-14 (III);gly-12 gly-13 (X)(III 和 X 指染色体编号)中均具有无效突变的蠕虫。三重敲除 (TKO) 线虫具有正常表型,尽管它们不表达 GnT I 活性,并且不合成野生型线虫中存在的 31 种寡甘露糖、复合物和岩藻糖基化寡甘露糖 N-聚糖。 TKO 蠕虫的非岩藻糖基化寡甘露糖 N-聚糖结构数量增加,这一发现与 GnT I 作用位点一致。在 TKO 线虫中观察到五种岩藻糖基化低聚甘露糖 N-聚糖结构,但在野生型线虫中未观察到,表明存在不寻常的 GnT I 独立岩藻糖基转移酶。结论是野生型C.线虫产生大量 GnT I 依赖性 N-聚糖,这些聚糖对于实验室条件下的正常蠕虫发育不是必需的。 TKO 蠕虫可能更容易受到其他基因突变的影响,从而提供了一种鉴定与 GnT I 相互作用的基因的方法。
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.