...
首页> 外文期刊>The FEBS journal >Endoproteolytic processing of the mammalian prionglycoprotein family
【24h】

Endoproteolytic processing of the mammalian prionglycoprotein family

机译:哺乳动物糖蛋白家族的内切蛋白加工

获取原文
获取原文并翻译 | 示例
           

摘要

Cellular prion protein (PrPC) misfolds to form infectivity-associated scrapieprion protein and generates C-terminal fragments C1 and C2 in healthyand prion-infected animals. C1 cleavage occurs N-terminally of PrPC’shydrophobic domain, whereas the larger C2 fragment is generated bycleavage at the end of the octarepeat region. As the PrP-like proteins Doppeland Shadoo (Sho) have been reported to inhabit similar membraneenvironments as PrPC, we investigated endoproteolysis by using a panel ofmutant alleles. Doppel undergoes efficient in vivo cleavage at a C1 sitemapped to the start of the globular domain, which is a structurally similarcleavage site to that in PrPC. Sho is processed to C1 and C2 fragments,and proved refractory to mutagenesis to inactivate C1 cleavage. As a reciprocalproduct of C1 cleavage, Sho also engenders a metabolically stableN1 fragment with a C-terminus after its hydrophobic domain, an observationthat may account for N1’s association with membrane and/or cellularfractions in vitro and in vivo. Our data indicate that glycosylation statusand yet to be identified proteases modulate internal C1 and C2 proteolysisevents within the mammalian prion protein family.
机译:在健康和感染(病毒的动物中,细胞fold病毒蛋白(PrPC)错折叠形成与感染性相关的scrapieprion蛋白,并产生C端片段C1和C2。 C1裂解发生在PrPC疏水结构域的N端,而更大的C2片段是通过在八面体区域的末端裂解产生的。据报道,由于PrP样蛋白Doppeland Shadoo(Sho)居住在与PrPC类似的膜环境中,因此我们使用一组突变等位基因研究了内切蛋白水解。多普尔在映射到球状结构域起点的C1位点进行有效的体内切割,该位点在结构上与PrPC中的切割位点相似。 Sho被加工成C1和C2片段,并被证明对诱变具有抵抗力,可以使C1裂解失活。作为C1切割的倒数产物,Sho还产生了一个在疏水域后带有C端的代谢稳定的N1片段,这一发现可能解释了N1在体外和体内与膜和/或细胞组分的关系。我们的数据表明,糖基化状态和尚未确定的蛋白酶调节哺乳动物病毒蛋白家族内的内部C1和C2蛋白水解事件。

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