Please use this identifier to cite or link to this item: http://hdl.handle.net/11455/62951
標題: 真核生物核糖體蛋白L23a與L35的晶體結構解析與功能研究
Crystallographic Structural and Functional Studies of Eukaryotic Ribosomal Protein L23a and L35
作者: 劉俊宏
關鍵字: 基礎研究;L23a;生物科學類;L23a;L35;核糖體蛋白質;核糖體;真核生物轉譯作用;蛋白質晶體結構;X 光晶譜學;L35;Ribosomal protein;Ribosome;Eukaryotic translation;Proteincrystal structure;X-ray crystallography
摘要: 
L23a 與L35 蛋白位在核糖體上一處重要且演化上高度保留的位置。由於坐落於此,他們可以與新生胜肽鏈、訊息辨識顆粒、監護蛋白、以及蛋白質引導通道相互作用來調控蛋白質合成作用。儘管對於原核生物核糖體的結構與功能已累積相當多的研究,科學界卻仍不清楚真核生物核糖體如何聯合其他蛋白質來進行準確與快速的蛋白質合成作用。真核生物核糖體蛋白L23a 與L35 在尺度上明顯大於他們的原核生物同源蛋白。倘若真如同我們所認知的,核糖體的結構與功能在不同的物種間均是十分相似,那麼為何真核生物需要增加這些結構成分?或許這些多出的結構成分會協助真核生物來調控較原核生物細胞內更為複雜的蛋白質合成作用。為了提供更多的資訊來了解這兩個影響深重的核糖體蛋白在真核生物轉譯作用中扮演的角色,在本研究計劃中,我們將投入於:(1) 描繪出真核核糖體蛋白L23a 與L35 的立體結構;(2) 獲取L23a 與L35 多出的結構成分的原子層次精細影像;(3) 提供L23a·L35 複合體與監護蛋白NAC 相互作用的結構細部資訊;(4) 提供L23a·L35 複合體與訊息辨識顆粒相互作用的結構細部資訊;(5)提供結構資訊證據來釐清監護蛋白NAC 與訊息辨識顆粒間在L23a·L35 上的競合關係;(6) 提供可能的結構資訊來探究L23a·L35 複合體與蛋白質引導通道間的交互作用。為求達成以上目標,我們將著手解析出酵母菌(Saccharomyces cerevisiae) L23a·L35 複合體的晶體結構。此外,我們也將研究L23a·L35 與目前已知的這些核糖體結合蛋白間的複合體結構,以期獲得極具價值的資訊引導我們了解L23a 與L35 如何在一個繁雜的真核細胞環境中協助核糖體來精準調控這些蛋白質的功能。我們執行中的這項研究適切可行,而且我們深信這項研究將會顯著地提升科學界對於真核生物轉譯作用的分子機制的認知。

L23a and L35 reside in the important, conserved platform of ribosome. Possessing thisspecial location allows these two proteins interact with the nascent polypeptide chain, thesignal recognition particle, the chaperones, as well as the protein-conducting channel duringprotein synthesis. Despite the enormous progress in studies on the structure and function ofprokaryotic ribosomes, the respective molecular details of the mechanism by which theeukaryotic ribosome and associated factors construct a polypeptide accurately and rapidly stillremain largely unexplored. Eukaryotic L23a and L35 are significantly larger in size than theireubacterial homologs. As the tertiary structure and function of the ribosome are conserved,what is the role of these additional components? One can image extra structure mayparticipate in mechanisms that eukaryotes have developed to regulate protein synthesis in amore complex fashion compared to prokaryotes. To provide more knowledge on the roles ofthese two influential ribosomal proteins in eukaryotes, in this research proposal we would liketo participate as follows: (1) To delineate the overall structural architectures of eukaryoticL23a and L35; (2) To obtain atomic resolution pictures of the structural extensions oneukaryotic L23a and L35, which are absent in their prokaryotic homolog; (3) To provide thestructural detail on interaction between L23aL35 with the ribosome-associated chaperone,NAC; (4) To provide the structural detail on interaction between L23aL35 with the signalrecognition particle; (5) To provide the structural clues to clarify the sharing or competingrelationship between NAC and the signal recognition particle on L23aL35; (6) To providepossible structural information on interaction between L23aL35 with the protein-conductingchannel. Towards the goals listed above, we are going to determine the crystal structure ofL23aL35 from yeast Saccharomyces cerevisiae. We will also conduct structural investigationon L23aL35 complexed with those known ribosome-associated proteins to provide valuableinsight into studying how L23a and L35 arrange such many factors simultaneously andsmoothly in a crowd and busy environment. This will be a promising approach and significantprogress will be achieved toward understanding the mechanisms of eukaryotic translation.
URI: http://hdl.handle.net/11455/62951
其他識別: NSC97-2311-B005-001-MY2
Appears in Collections:生物科技發展中心

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