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Biochemical and Functional Characterization of Pollen-Predominant CDPKs and a Downstream Substrate in Rice
Calcium-dependent Protein Kinase
Oryza sativa L.
RuvB-like DNA Helicase
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實驗室先前利用差異性選殖方式篩選出主要於花粉成熟時期表現之基因，命名為 OsCPK26 (Oryza sativa calcium-dependent protein kinase 26)，以酵母菌雙雜交法篩選出OsCPK26之下游受質蛋白，篩選出一個結合蛋白命名為OIP30 (OsCPK26-interacting protein)，經序列比對發現OIP30為RuvB-like DNA 2解旋酶，OIP30受OsCPK26磷酸化後，其解旋酶及ATP水解酶的活性皆提升約三倍之多。本實驗分析OIP30與OsCPK26於百合花粉管次細胞之分布，利用超高速離心將水稻成熟花粉之初萃液區分為soluble 及membrane 部分，以西方墨點法偵測，發現成熟花粉中之OIP30與OsCPK26皆位於membrane 部分，進一步利用點突變將OsCPK26 蛋白N端的荳蔻酸訊號進行G2A突變，使OsCPK26失去荳蔻酸之修飾作用，結果證實荳蔻酸為OsCPK26蛋白附著在膜上的主要因素。以螢光蛋白標定方式追蹤，OsCPK26位於細胞膜上而OIP30位於細胞質中，兩種蛋白共表現時，則其訊號均位於細胞膜上；進而利用不活化型之OsCPK26(CI) 代替活化型 OsCPK26 (wild type) ，發現OsCPK26(CI) 與OIP30也共分佈於細胞膜上，但明顯不同的是OIP30與OsCPK26(CI)的訊號完全重疊，這與OsCPK26(wt) 與OIP30訊號並非完全重疊的現象明顯不同，猜測可能是磷酸化反應後造成OsCPK26/OIP30複合體構型改變所致。進一步利用OsCPK26(G2A) 突變型與OIP30共表現於百合花粉管中進行觀察，當OsCPK26(G2A)或OIP30單獨表現時，此二蛋白皆位於細胞質，若OsCPK26(G2A) 與OIP30共表現，則此二蛋白明顯共同進入細胞核內，有趣的是，OsCPK26於C端具明顯的進核訊號 (NLS) ，雖有明顯進核訊號，但不論是活化型、非活化型或是G2A突變型之OsCPK26皆無法單獨進入花粉管核內，必需是以G2A突變型蛋白與OIP30蛋白結合後，方能進入花粉管核，這暗示著OIP30為OsCPK26進核的必要條件。
鈣離子是調控花粉萌發之必要因素，故CDPK (calcium-dependent calmodulin-independent protein kinase) 基因與調控花粉萌發及花粉管之延長的過程有關。先前實驗室利用酵母菌雙雜交法，篩選可能為OsCPK25/26的結合蛋白或下游受質蛋白，意外發現有兩個OsCPK蛋白，分別為OsCPK21與OsCPK29，這兩個CDPK皆主要表現於水稻成熟花粉中；由酵母菌雙雜交法篩選到兩個CDPK基因，這暗示著CDPK形成複合體的可能性。OsCPK2、OsCPK25/26與OsCPK29皆主要表現於水稻成熟花粉中，故探討水稻成熟花粉中CDPK形成複合體的可能性；依據水稻基因組資料庫的資訊，設計引子進行RT-PCR，將主要表現於水稻成熟花粉之CDPK皆選殖出，共得到六個OsCPK全長cDNA基因，一一配對進行酵母菌雙雜交測試，結果發現除了OsCPK25/26沒有之外其他CDPKs皆與OsCPK2有交互結合現象，因此選擇花粉中表達量較高的OsCPK2與OsCPK29進行實驗。以免疫共沉澱實驗中發現OsCPK2與OsCPK29可形成複合體，且鈣離子為形成複合體之必要因素；進一步以受質磷酸化實驗觀察複合體之活性，發現複合體之磷酸激酶活性上升，甚至以CI (catalytic inactive form) 與wt CDPK融合蛋白配對之受質磷酸化實驗，同樣可觀察到複合體之活性上升。Chandran (2006) 分析蛋白結晶結構指出 AtCPK1 之J-CaML可形成雙聚體，其中之F436 會坐落於C-lobe中，為形成雙聚體之主要結合力量，利用ClustalW程式比對OsCPK2、OsCPK29與AtCPK1之J-CaML胺基酸序列，比對結果發現與AtCPK1與OsCPK29相似度有60%、與OsCPK2相似度高達73%，比對序列中發現OsCPK2之F347與OsCPK29之F370對應於AtCPK1之F436，進一步利用Swiss-Model軟體模擬出OsCPK2及OsCPK29之立體結構，結構比對發現OsCPK2之F347與OsCPK29之F370同樣皆會落在C-lobe口袋中，此與AtCPK1結晶觀察結論相同；由in vitro及in vivo實驗果顯示，OsCPK2與OsCPK29可形成複合體，且複合體之活性有提升之現象。|
Chapter 1 Calcium ion is a well-known essential component for pollen germination and tube elongation. Several calcium-dependent protein kinases (CDPKs) are expressed predominantly in mature pollen grains and play a critical role in pollen. However, none of their interacting proteins or downstream substrates have been identified. Using yeast two-hybrid screening, we isolated OsCPK25/26-interacting protein 30 (OIP30), which is also predominantly expressed in pollen. OIP30 encodes a RuvB-like DNA helicase 2 (RuvBL2) that is well conserved in eukaryotic species from yeast to human. Yeast and Drosophila defective in RuvBL2 are nonviable. The interaction between OsCPK26 and OIP30 was confirmed by far-western blot and pull-down experiments. OIP30 was phosphorylated in a calcium-dependent manner by OsCPK26 but not OsCPK2, which is highly similar to OsCPK26 in sequence and expression profile. OIP30 unwound partial duplex DNA with a 3''to 5''directionality by ATP hydrolysis. Concurrently, the ATPase activity of OIP30 depended on single-stranded DNA. OsCPK26 phosphorylated OIP30 and enhanced both its helicase and ATPase activity about threefold. OIP30 may be the potential downstream substrate for OsCPK25/26 in pollen. This report characterizes a RuvBL in plants and links its activities with its upstream regulator. Chapter 2 OIP30, a RuvB-like DNA helicase 2, was identified as downstream substrate for OsCPK26, a calcium-dependent protein kinase (CDPK) that expressed predominantly in mature pollen of rice. OsCPK26 phosphorylated OIP30 and enhanced both its helicase and ATPase activity about threefold. In this report, we characterized subcellular distributions of these two proteins in germinating lily pollen. In the mature pollen grain of rice, both OsCPK26 and OIP30 were found to be located predominantly in membrane fraction. A G2A mutation demonstrated that the N-terminal myristoyl modification of OsCPK26 is essential for membrane anchorage of both OsCPK26 and OIP30. In contrast to the catalytically inactive (CI) OsCPK26 that seem to lock OIP30, protein signals of wild type OsCPK26 and OIP30 were not fully overlapped on membrane, implicating that kinase reaction may relax their complex conformation. Moreover, for OIP30 to act as a DNA helicase, a nuclear targeting is required. Using OsCPK26(G2A) mutant to bypass the membrane anchorage, we found that both OsCPK26(G2A) and OIP30 remained in cytoplasm if expressed alone, but highly co-localized in nucleus if co-expressed. Interestingly, beside a bipartite nuclear localization signal (NLS) at the C-terminus of OsCPK26, kinase activity was also found to be crucial for nuclear import of the OsCPK26/OIP30 complex. There seem to be a tight regulation which only allows the active OsCPK26/OIP30 complex to enter nucleus in pollen tube. Chapter 3 Calcium is well known to play critical roles in pollen germination and tube elongation. Calcium-dependent calmodulin-independent protein kinases (CDPKs) that expressed predominantly in mature pollen may be responsible for transducing calcium signals to downstream substrates in pollen. Using the yeast two-hybrid (Y2H) in substrate hunting, we were surprised to find two CDPKs, OsCPK21 and OsCPK29, strongly interacted with bait protein, the kinase domain of OsCPK25/26. RT-PCR examinations revealed that OsCPK21 and OsCPK29 were also expressed predominantly in pollen, implicating possibility of complex formation between different CDPKs in pollen. A systematic survey of the seven pollen-predominant OsCPKs by Y2H showed various interactions among different OsCPKs, with OsCPK2 exhibited the most prominent affinities with all other OsCPKs, except for OsCPK25/26. OsCPK2 and OsCPK29 were chosen for further studies of their protein-protein interactions. Pull-down experiments using OsCPK29-HA and c-myc-OsCPK2 that co-expressed in tobacco leaf demonstrated possibility of their complex formation in plant cell. Moreover, calcium ion is required for this protein complex as EGTA dissociate it. As synergistic effects were observed for kinase activities of recombinant OsCPK2 and OsCPK29 when co-incubated, we suspected that it may be caused by heterocomplex formation between two proteins. To simplify assay, we use catalytic inactive (CI) OsCPKs instead. Interestingly, constant amount of OsCPK exhibited enhanced activities that proportional to the increasing amount of OsCPK(CI) in assay, suggesting that complex formation between CDPKs may stimulate its kinase activity in a phosphorylation-independent manner.
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