• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Molecular and Cellular Biology >Prolyl 4-Hydroxylase Is an Essential Procollagen-Modifying Enzyme Required for Exoskeleton Formation and the Maintenance of Body Shape in the Nematode Caenorhabditis elegans
【24h】

Prolyl 4-Hydroxylase Is an Essential Procollagen-Modifying Enzyme Required for Exoskeleton Formation and the Maintenance of Body Shape in the Nematode Caenorhabditis elegans

机译：Prolyl 4-羟化酶是线虫秀丽隐杆线虫外骨骼形成和维持体形所需的必需的胶原蛋白修饰酶。

获取原文
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

The multienzyme complex prolyl 4-hydroxylase catalyzes the hydroxylation of proline residues and acts as a chaperone during collagen synthesis in multicellular organisms. The β subunit of this complex is identical to protein disulfide isomerase (PDI). The free-living nematode Caenorhabditis elegans is encased in a collagenous exoskeleton and represents an excellent model for the study of collagen biosynthesis and extracellular matrix formation. In this study, we examined prolyl 4-hydroxylase α-subunit (PHY; EC1.14.11.2)- and β-subunit (PDI; EC 5.3.4.1)-encoding genes with respect to their role in collagen modification and formation of theC. elegans exoskeleton. We identified genes encoding two PHYs and a single associated PDI and showed that all three are expressed in collagen-synthesizing ectodermal cells at times of maximal collagen synthesis. Disruption of the pdi gene via RNA interference resulted in embryonic lethality. Similarly, the combinedphy genes are required for embryonic development. Interference with phy-1 resulted in a morphologically dumpy phenotype, which we determined to be identical to the uncharacterizeddpy-18 locus. Two dpy-18 mutant strains were shown to have null alleles for phy-1 and to have a reduced hydroxyproline content in their exoskeleton collagens. This study demonstrates in vivo that this enzyme complex plays a central role in extracellular matrix formation and is essential for normal metazoan development.
机译：多酶复合物脯氨酰4-羟化酶催化脯氨酸残基的羟化作用，并在多细胞生物体的胶原合成过程中充当分子伴侣。该复合物的β亚基与蛋白质二硫键异构酶（PDI）相同。自由生活的线虫秀丽隐杆线虫包裹在胶原外骨骼中，代表了研究胶原生物合成和细胞外基质形成的极佳模型。在这项研究中，我们检查了脯氨酰4-羟化酶α亚基（PHY; EC1.14.11.2）和β亚基（PDI; EC 5.3.4.1）编码基因在胶原蛋白修饰和形成过程中的作用。 C。线虫外骨骼。我们鉴定了编码两个PHY和一个相关的PDI的基因，并显示在胶原合成最大的时候，所有三个都在合成胶原的外胚层细胞中表达。通过RNA干扰破坏 pdi 基因会导致胚胎致死。同样，组合的 phy 基因是胚胎发育所必需的。干扰 phy-1 会导致形态上笨拙的表型，我们确定该表型与未表征的 dpy-18 基因座相同。结果显示，两个 dpy-18 突变菌株的 phy-1 等位基因无效，外骨骼胶原蛋白中的羟脯氨酸含量降低。这项研究在体内证明了这种酶复合物在细胞外基质形成中起着核心作用，对于正常的后生动物发育至关重要。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号