臺灣博碩士論文加值系統

(一) 細菌染色體的複製需要利用引子合成體 (Primosome) 來引導 DNA 的合成，而PriB是構成大腸桿菌 (Escherichia coli) 內fX型引子合成體 (fX-type primosome) 的重要蛋白質之一。體外實驗顯示PriB能與單股DNA，單股RNA或其他染色體複製相關蛋白相結合。本論文探討大腸桿菌引子合成體蛋白PriB的晶體結構。此結構是利用多波長反常散射法 (Multi-wavelength anomalous diffraction) 解出，並擁有2.1 Å的解析度。PriB蛋白質的單體結構形似單股DNA結合蛋白 (Single-stranded DNA-binding Protein) 的DNA結合區，然而PriB在細胞內是以雙倍體型式執行其功能，而非如同單股DNA結合蛋白在細胞內為四倍體。利用此次解出的結構資訊，與現有的生化研究結果相結合，我們推斷出PriB可能利用其表面的若干特定區域，在引子合成體組成時與DNA，RNA或其他蛋白質相結合。這些發現將有助於我們了解PriB在細菌染色體複製時所扮演的角色。
(二) 許多研究發現位在細胞表面的醣神經胺醇脂 (Glycosphingolipids) 在細胞間的辨識機制上扮演重要角色。例如，細菌、病毒或毒素蛋白會透過它們來入侵細胞。眼鏡蛇咬傷患者會受到心臟毒素 (Cardiotoxins) 的侵害，導致嚴重的組織壞死與心臟收縮停止。心臟毒素為一群同源且結構相似的鹼性胜肽，其性質類似細胞穿透胜肽 (Cell-penetrating peptides)，能與細胞膜脂質和肝素 (Heparin) 結合。目前認為，當受到肝素的吸引而聚集到受害者細胞表面，心臟毒素的親脂活性可能導致細胞膜泄漏而殺死細胞。近期研究顯示台灣眼鏡蛇心臟毒素中的主要蛋白，心臟毒素A3，會結合細胞外膜的硫醣苷脂 (Sulfatide)，藉助於硫醣苷脂導致細胞膜泄漏，並近一步入侵細胞內的粒腺體。硫醣苷脂為帶有硫酸半乳糖基的醣神經胺醇脂。本論文探討眼鏡蛇心臟毒素A3/硫醣苷脂複合體的晶體結構。此複合體晶體生長於類似細胞膜的疏水環境，並擁有2.3 Å的解析度。晶體結構顯示，心臟毒素A3能同時辨識硫醣苷脂上的頭部官能基以及神經醯胺 (Ceramide) 官能基部位的親水親油介面區，而硫醣苷脂在與心臟毒素A3結合後，改變了原有的構形。利用此次解出的結構資訊與現有的研究結果相結合，我們推論在兩者相結合後的脂質構形變化使得心臟毒素A3穿透細胞膜，並且以多倍體方式聚合而進入細胞。現今生物醫學領域廣泛研究利用細胞穿透胜肽來投遞癌症治療用DNA或蛋白質的方法，然而其細胞穿透的分子機制依然懸而未解。有鑑於心臟毒素A3和細胞穿透胜肽間在化學組成與對細胞的生理功能上十分相似，我們期盼提出此種藉由脂質引導蛋白毒素穿透細胞膜的機制有助於更了解細胞穿透胜肽的穿透機制。

(1) PriB is one of the Escherichia coli phiX-type primosome proteins, which are required for assembly of the primosome, a mobile multi-enzyme complex responsible for the initiation of DNA replication. Here we report the crystal structure of the Escherichia coli PriB at 2.1 Å resolution by multi-wavelength anomalous diffraction using a mercury derivative. The polypeptide chain of PriB is structurally similar to that of single-stranded DNA-binding protein (SSB). However, the biological unit of PriB is a dimer, not a homotetramer like SSB. Electrophoretic mobility shift assays demonstrated that PriB binds single-stranded DNA and single-stranded RNA with comparable affinity. We also show that PriB binds single-stranded DNA with certain base preferences. Base on the PriB structural information and biochemical studies, we propose that the potential tetramer formation surface and several other regions of PriB may participate in protein-protein interaction during DNA replication. These findings may illuminate the role of PriB in phiX-type primosome assembly.
(2) Cobra cardiotoxins, a family of basic polypeptides having lipid- and heparin-binding capacities similar to the cell-penetrating peptides, induce severe tissue necrosis and systolic heart arrest in snakebite victims. While cardiotoxins are specifically retained on the cell surface via heparin-mediated processes, their lipid binding ability appears to be responsible, at least in part, for cardiotoxin-induced membrane leakage and cell death. Recent studies showed that CTX A3, the major cardiotoxin from Taiwan cobra venom, binds to sulfatide in the outer leaflet of the plasma membrane, and consequently sulfatide mediates CTX A3-induced membrane leakage and CTX A3 internalization into mitochondria. Sulfatide is a glycosphingolipid with 3'-sulfated galactose headgroup. Here we describe the crystal structure of a CTX A3/sulfatide complex in a membrane-like environment at 2.3 Å resolution. The unexpected orientation of the sulfatide fatty chains in the structure allows prediction of the mode of toxin insertion into the plasma membrane. CTX A3 recognizes both the headgroup and the ceramide interfacial region of sulfatide to induce a lipid conformational change that may play a key role in CTX A3 oligomerization and cellular internalization. This proposed lipid-mediated toxin translocation mechanism may also shed light on the cellular uptake mechanism of the amphiphilic cell-penetrating peptides known to involve multiple internalization pathways.

Volume 1: Crystal structure of PriB, a primosomal DNA replication protein of Escherichia coli.

Chapter 1: Introduction ………………………………… 1
Chapter 2: Material and methods ………………………………… 5
Chapter 3: Results and discussion ………………………………… 13
Chapter 4: Conclusion ………………………………… 24
References ………………………………… 40

Volume 2: Structural basis of glycosphingolipid-facilitated cobra cardiotoxin A3 membrane insertion and internalization: crystal structure of cardiotoxin A3/sulfatide complex.

Chapter 1: Introduction ………………………………… 48
Chapter 2: Material and methods ………………………………… 59
Chapter 3: Results ………………………………… 66
Chapter 4: Discussion ………………………………… 70
Chapter 5: Conclusion ………………………………… 76
References ………………………………… 94

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