hUFP基因功能研究
發(fā)布時(shí)間:2018-07-25 16:26
【摘要】:目前,越來越多的證據(jù)表明,真核細(xì)胞內(nèi)大部分的蛋白質(zhì)都是通過ATP依賴的泛素/蛋白酶體通路(Ubiquitin/proteosome pathway,UPP)降解的。UPP由一系列的蛋白質(zhì)組成,,包括泛素、泛素連接酶、去泛素化酶以及蛋白酶體,主要存在于細(xì)胞核、細(xì)胞質(zhì)中,也存在于細(xì)胞膜上,能選擇性地降解細(xì)胞內(nèi)變性、變構(gòu)或錯(cuò)誤翻譯的蛋白以及各種調(diào)節(jié)蛋白等,因而在細(xì)胞周期的控制、免疫應(yīng)答、脅迫反應(yīng)和細(xì)胞程序性死亡等許多細(xì)胞內(nèi)基本生理過程中起重要作用。 泛素(Ubiquitin)是含有76個(gè)氨基酸殘基的低分子量蛋白質(zhì),序列極其保守。近來很多研究表明,真核細(xì)胞中有大量的基因與泛素有較高的同源性,或者沒有同源性但是確有相似的功能。它們獨(dú)立形成了巨大的“蛋白質(zhì)翻譯后修飾系統(tǒng)”。這些泛素樣蛋白根據(jù)其與泛素的同源性和功能的不同,可分為泛素樣修飾蛋白(ubiquitin-like modifiers,UBLs)和泛素域樣蛋白(ubiquitin-domain proteins,UDPs)兩類。研究表明UDPs不參與泛素/蛋白酶體通路,不具備對蛋白質(zhì)行使修飾的能力。而UBLs則行使泛素樣修飾作用,但初步研究認(rèn)為其并非發(fā)揮蛋白
[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.
【學(xué)位授予單位】:南京醫(yī)科大學(xué)
【學(xué)位級別】:博士
【學(xué)位授予年份】:2006
【分類號】:R346
本文編號: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.
【學(xué)位授予單位】:南京醫(yī)科大學(xué)
【學(xué)位級別】:博士
【學(xué)位授予年份】:2006
【分類號】:R346
【參考文獻(xiàn)】
相關(guān)碩士學(xué)位論文 前1條
1 魯可可;人類hUFP基因初步研究[D];南京醫(yī)科大學(xué);2004年
本文編號:2144389
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