hUFP基因功能研究
发布时间：2018-07-25 16:26
【摘要】：目前，越来越多的证据表明，真核细胞内大部分的蛋白质都是通过ATP依赖的泛素／蛋白酶体通路(Ubiquitin／proteosome pathway，UPP)降解的。UPP由一系列的蛋白质组成，，包括泛素、泛素连接酶、去泛素化酶以及蛋白酶体，主要存在于细胞核、细胞质中，也存在于细胞膜上，能选择性地降解细胞内变性、变构或错误翻译的蛋白以及各种调节蛋白等，因而在细胞周期的控制、免疫应答、胁迫反应和细胞程序性死亡等许多细胞内基本生理过程中起重要作用。 泛素(Ubiquitin)是含有76个氨基酸残基的低分子量蛋白质，序列极其保守。近来很多研究表明，真核细胞中有大量的基因与泛素有较高的同源性，或者没有同源性但是确有相似的功能。它们独立形成了巨大的“蛋白质翻译后修饰系统”。这些泛素样蛋白根据其与泛素的同源性和功能的不同，可分为泛素样修饰蛋白(ubiquitin-like modifiers，UBLs)和泛素域样蛋白(ubiquitin-domain proteins，UDPs)两类。研究表明UDPs不参与泛素／蛋白酶体通路，不具备对蛋白质行使修饰的能力。而UBLs则行使泛素样修饰作用，但初步研究认为其并非发挥蛋白
[Abstract]:At present, there is increasing evidence that most of the proteins in eukaryotic cells are degraded through the ATP dependent Ubiquitin/proteosome path / proteasome pathway (UPP), which consists of a series of proteins, including ubiquitin, ubiquitin ligase. De-ubiquitin enzymes and proteasome, mainly found in the nucleus, cytoplasm and cell membrane, can selectively degrade intracellular denaturation, mutagenesis or mistranslation of proteins, as well as various regulatory proteins, etc. Therefore, it plays an important role in many basic cellular physiological processes, such as cell cycle control, immune response, stress response and programmed cell death. Ubiquitin (Ubiquitin) is a low molecular weight protein with 76 amino acid residues. Recent studies have shown that a large number of genes in eukaryotic cells have high homology or no homology but do have similar functions. They independently form a huge "protein post-translational modification system". According to their homology and function, these ubiquitin like proteins can be divided into two groups: ubiquitin-like modifiers (UBLs) and ubiquitin-domain proteins (UDPs). UDPs does not participate in the ubiquitin / proteasome pathway and does not have the ability to modify proteins. However, UBLs acts as a ubiquitin like modifier, but preliminary studies suggest that it does not play a role in protein.
【学位授予单位】：南京医科大学
【学位级别】：博士
【学位授予年份】：2006
【分类号】：R346
本文编号：2144389
[Abstract]:At present, there is increasing evidence that most of the proteins in eukaryotic cells are degraded through the ATP dependent Ubiquitin/proteosome path / proteasome pathway (UPP), which consists of a series of proteins, including ubiquitin, ubiquitin ligase. De-ubiquitin enzymes and proteasome, mainly found in the nucleus, cytoplasm and cell membrane, can selectively degrade intracellular denaturation, mutagenesis or mistranslation of proteins, as well as various regulatory proteins, etc. Therefore, it plays an important role in many basic cellular physiological processes, such as cell cycle control, immune response, stress response and programmed cell death. Ubiquitin (Ubiquitin) is a low molecular weight protein with 76 amino acid residues. Recent studies have shown that a large number of genes in eukaryotic cells have high homology or no homology but do have similar functions. They independently form a huge "protein post-translational modification system". According to their homology and function, these ubiquitin like proteins can be divided into two groups: ubiquitin-like modifiers (UBLs) and ubiquitin-domain proteins (UDPs). UDPs does not participate in the ubiquitin / proteasome pathway and does not have the ability to modify proteins. However, UBLs acts as a ubiquitin like modifier, but preliminary studies suggest that it does not play a role in protein.
【学位授予单位】：南京医科大学
【学位级别】：博士
【学位授予年份】：2006
【分类号】：R346
【参考文献】
相关硕士学位论文 前1条
1 鲁可可;人类hUFP基因初步研究[D];南京医科大学;2004年
本文编号：2144389
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