博碩士論文 102224007 詳細資訊




以作者查詢圖書館館藏 以作者查詢臺灣博碩士 以作者查詢全國書目 勘誤回報 、線上人數:35 、訪客IP:18.221.179.220
姓名 鍾岳霖(Yue-Lin Chung)  查詢紙本館藏   畢業系所 生命科學系
論文名稱 探討OsCCR4a 與 OsCCR4b兩個水稻CCR4同源蛋白之去腺苷酸酵素活性
(Studying on deadenylation capabilities of two homologous rice carbon catabolite repression 4 proteins, OsCCR4a and OsCCR4b)
相關論文
★ 水稻CAF1基因之功能分析-水稻CAF1基因的選殖、定性及表現★ 水稻OsDEADl-1基因的功能性探討
★ 利用水稻細胞之懸浮培養建立蛋白質高效率分泌系統★ 水稻CCR4基因之功能分析- 水稻CCR4基因的選殖、定性及表現
★ 阿拉伯芥 AtMYBS 基因功能性探討★ 水稻OsMYBS2基因的功能性分析
★ 水稻CCR4基因的功能分析- 繁衍大量表現和靜默表現的基因轉殖水稻★ 水稻OsVALs基因的功能性分析- 水稻OsVALs基因的選殖、定性及表現
★ 分析水稻T-DNA插入突變株: M0022150, M0023563, M0023580, M0037352及M0032079★ 以水稻懸浮培養細胞蛋白質生產系統生產mGMCSF
★ 建立表現耐熱澱粉普魯南糖酶基因之轉植甘藷★ 阿拉伯芥AtMYBSs基因參與在糖訊息及離層酸訊息傳遞之研究
★ I. II.★ 探討αAmy3、OsCIN1與Os33KD信號肽在水稻懸浮培養細胞中的功能及特性
★ 水稻CAF1基因在水稻懸浮培養細胞之研究★ 探討阿拉伯芥兩個MYB-related轉錄因子在糖訊息傳遞中所扮演的角色
檔案 [Endnote RIS 格式]    [Bibtex 格式]    [相關文章]   [文章引用]   [完整記錄]   [館藏目錄]   至系統瀏覽論文 ( 永不開放)
摘要(中) 從單細胞酵母菌一直到多細胞動物,如:老鼠、人類等真核生物中都具有CCR4-NOT複合體,這個複合體對於基因表達是整體的調節者。複合體中的各個蛋白質對於不同層面的mRNA代謝都有關聯,包括transcription initiation、elongation 和mRNA degradation。控制mRNA的半衰期是調控基因表現的重要一環,大部分的情況下,調控真核細胞mRNA半衰期的主要途徑是先將mRNA的poly (A) tail縮短。在酵母菌的研究得知,CCR4蛋白質是CCR4-NOT複合體的其中一個成員,並已經證實在細胞質中具有deadenylation的功能。然而,水稻CCR4的功能目前尚未清楚,因此本篇論文將進一步探討CCR4在水稻中的功能。
透過胺基酸序列比對分析發現兩個水稻CCR4 homolog,並命名為OsCCR4a和OsCCR4b。水稻CCR4的C端nuclease domain重組蛋白質:His-OsCCR4a EEP 和His-OsCCR4b EEP,在in vitro的實驗中證實具有deadeanylase的酵素活性,在水稻CCR4的activity site點突變會使其deadeanylase的酵素活性消失。processing bodies是存在真核細胞的細胞質中顆粒狀結構,裡面包含了很多跟mRNA turnover有關的酵素,我們發現水稻CCR4會在細胞質的processing bodies中。基因表現的部分,發現OsCCR4a和OsCCR4b基因在葉子和劍葉的部分表現量比較高,並且會受到熱逆境所誘導,但是在賀爾蒙2,4D以及NAA的處理下,OsCCCR4b會被誘導而OsCCR4a的基因表現不會受到影響。兩個OsCCR4蛋白質都具有deadenylase的酵素活性,並且會在細胞質的processing bodies中,推測OsCCR4蛋白質可能參與水稻中 mRNA的deadeylation;從基因表現的部分,發現在水稻發育過程或受到環境壓力下OsCCR4a和OsCCR4b並不是完全的functional redundancy。
摘要(英) The CCR4-NOT (carbon catabolite repression, negative on TATA-less) complex is a global regulator of gene expression that is conserved from yeast to human. The complex is involved in several aspects of mRNA metabolism, including transcription initiation, elongation and mRNA degradation. Control of mRNA turnover is a critical mechanism for regulating of gene expression in eukaryotice cells. One of major pathway of mRNA turnover in eukaryotic cells is initiated by mRNA deadenylation (also called as poly(A) tail shortening). In yeast, the CCR4 protein, as part of the CCR4-NOT complex, has been shown that take a responsibility for cytoplasmic deadenylation. However, the function of CCR4 in rice is not clear yet. In this study, we identified and cloned two CCR4 homologs, OsCCR4a and OsCCR4b, from Oryza sativa. The OsCCR4s C-terminal nuclease domain recombinant proteins, His-OsCCR4a EEP and His-OsCCR4b EEP, exhibited deadenylase activity in vitro, and mutation in their activity site abolished their deadenylase activities, respectively. Subcellular localization analysis showed that OsCCR4a-GFP and OsCCR4b-GFP are localized in cytoplasmic mRNA processing bodies (P-bodies), which are specific granules consisting of enzymes involved in mRNA turnover. Both OsCCR4s were suggested are heat stress related genes while their expression were induced by heat stress in rice. However, only OsCCR4b was induced by 2,4D and NAA treatments. Our findings provide biochemical evidence that two OsCCR4 proteins may be involved in the deadenylation in rice. The various expression patterns between two OsCCR4s implied that OsCCR4a and OsCCR4b aren’t completely functional redundancy in the developmental process and stress response of the rice.
關鍵字(中) ★ mRNA的降解
★ CCR4-NOT複合體
★ 去腺苷酸酵素
關鍵字(英) ★ mRNA
★ Deadenylase
★ CCR4-NOT complex
論文目次 目錄
摘要 I
Abstract II
目錄 III
壹、 序論 1
1. mRNA數量的調控機制 1
2. mRNA的降解 2
3. Deadenylase 4
4. CCR4-NOT complex 6
5. CCR4 7
6. Processing bodies 12
7. OsCCR4 14
貳、 材料與方法 15
1. CCR4同源性基因的鑑定與親緣關係樹的分析 15
1.1 CCR4同源性基因的鑑定 15
1.2 CCR4同源性基因的序列比對與親緣關係樹的建立 15
2. cDNA的製備 15
2.1 製備DEPC-treated ddH2O (RNase-free)溶液 15
2.2 萃取Total RNA 15
2.3 去除染色體DNA之汙染 16
2.4 cDNA之合成 16
3. 質體的建構 16
3.1 設計引子 16
3.2 利用PCR合成水稻CCR4基因片段 17
3.3 水稻CCR4基因點突變片段的合成 17
3.4 瓊脂膠體回收DNA 18
3.5 DNA片段接合至T&A載體中 18
3.6 蛋白質表達質體的建構 19
3.7 螢光蛋白融合OsCCR4s表達質體的建構 19
4. 細菌的轉型作用 19
4.1 製備E. coli competent cell (DH5α strain,BL21 strain) 19
4.2 細菌的轉型(transformation) 20
4.3 小量純化細菌質體DNA 20
5. 水稻原生質體的轉型方法 21
5.1 水稻植株的培養 21
5.2 原生質體製備 (protoplast isolation) 21
5.3 PEG transformation 22
6. 洋蔥表皮細胞利用微粒子投射法(particle bombardment)的轉型 22
6.1 洋蔥表皮細胞的準備 22
6.2 基因槍設定 22
6.3 金粒子的製備 23
6.4 DNA附著 23
6.5 轉型樣品處理 23
7. 蛋白質的表達與純化 23
7.1 利用E. coli表達目標蛋白質 23
7.2 蛋白質表達 23
7.3 蛋白質萃取 24
7.4 蛋白質純化 24
7.5 蛋白質電泳(SDS-PAGE) 25
7.6 西方墨點法 25
7.7 蛋白質濃縮以及濃度測定 26
8. In vitro deadenylase活性測試 26
8.1 受質RNA設計 26
8.2 活性測試 26
8.3 RNA電泳 27
9. 在逆境下OsCCR4s基因表現之分析 27
9.1 水稻植株的培養 27
9.2 逆境的處理 27
9.3 基因表現的分析 27
參、 實驗結果 29
1. 水稻CCR4同源性基因的鑑定與親緣關係樹的分析 29
2. 水稻CCR4同源性蛋白質胺基酸序列比對分析 29
3. OsCCR4s蛋白質結構預測 30
4. OsCCR4s蛋白質的表達與純化 31
5. OsCCR4s的deadenylase活性測試 33
6. OsCCR4s在細胞中的位置 34
7. OsCCR4s與OsCAF1s基因在水稻不同組織中以及受到環境壓力時的表現 35
肆、 討論 37
1. CCR4同源性基因的鑑定與親緣關係樹的分析 37
2. 水稻CCR4同源性蛋白質胺基酸序列比對分析與蛋白質結構預測 38
3. 水稻CCR4蛋白質的表達與純化 39
4. 水稻CCR4的deadenylase活性測試 39
5. 水稻CCR4在細胞中的位置 40
6. 水稻CCR4基因在水稻不同組織中以及受到環境壓力時的表現 41
伍、 參考資料 43
陸、 圖表 55
柒、 附錄 94
參考文獻 Uncategorized References
Albert, T.K., Lemaire, M., van Berkum, N.L., Gentz, R., Collart, M.A., and Timmers, H.T. (2000). Isolation and characterization of human orthologs of yeast CCR4-NOT complex subunits. Nucleic Acids Res 28, 809-817.
Anderson, P., and Kedersha, N. (2006). RNA granules. J Cell Biol 172, 803-808.
Ansieau, S., and Leutz, A. (2002). The conserved Mynd domain of BS69 binds cellular and oncoviral proteins through a common PXLXP motif. J Biol Chem 277, 4906-4910.
Assenholt, J., Mouaikel, J., Saguez, C., Rougemaille, M., Libri, D., and Jensen, T.H. (2011). Implication of Ccr4-Not complex function in mRNA quality control in Saccharomyces cerevisiae. RNA 17, 1788-1794.
Azzouz, N., Panasenko, O.O., Colau, G., and Collart, M.A. (2009). The CCR4-NOT complex physically and functionally interacts with TRAMP and the nuclear exosome. PLoS One 4, e6760.
Badis, G., Saveanu, C., Fromont-Racine, M., and Jacquier, A. (2004). Targeted mRNA degradation by deadenylation-independent decapping. Mol Cell 15, 5-15.
Baggs, J.E., and Green, C.B. (2003). Nocturnin, a deadenylase in Xenopus laevis retina: a mechanism for posttranscriptional control of circadian-related mRNA. Curr Biol 13, 189-198.
Bai, Y., Salvadore, C., Chiang, Y.C., Collart, M.A., Liu, H.Y., and Denis, C.L. (1999). The CCR4 and CAF1 proteins of the CCR4-NOT complex are physically and functionally separated from NOT2, NOT4, and NOT5. Mol Cell Biol 19, 6642-6651.
Balatsos, N.A., Nilsson, P., Mazza, C., Cusack, S., and Virtanen, A. (2006). Inhibition of mRNA deadenylation by the nuclear cap binding complex (CBC). J Biol Chem 281, 4517-4522.
Bashkirov, V.I., Scherthan, H., Solinger, J.A., Buerstedde, J.M., and Heyer, W.D. (1997). A mouse cytoplasmic exoribonuclease (mXRN1p) with preference for G4 tetraplex substrates. J Cell Biol 136, 761-773.
Basquin, J., Roudko, V.V., Rode, M., Basquin, C., Seraphin, B., and Conti, E. (2012). Architecture of the nuclease module of the yeast Ccr4-not complex: the Not1-Caf1-Ccr4 interaction. Mol Cell 48, 207-218.
Bhattacharyya, S.N., Habermacher, R., Martine, U., Closs, E.I., and Filipowicz, W. (2006). Relief of microRNA-mediated translational repression in human cells subjected to stress. Cell 125, 1111-1124.
Brengues, M., Teixeira, D., and Parker, R. (2005). Movement of eukaryotic mRNAs between polysomes and cytoplasmic processing bodies. Science 310, 486-489.
Brown, C.E., Tarun, S.Z., Jr., Boeck, R., and Sachs, A.B. (1996). PAN3 encodes a subunit of the Pab1p-dependent poly(A) nuclease in Saccharomyces cerevisiae. Mol Cell Biol 16, 5744-5753.
Chen, C.Y., and Shyu, A.B. (2011). Mechanisms of deadenylation-dependent decay. Wiley Interdiscip Rev RNA 2, 167-183.
Chen, J., Chiang, Y.C., and Denis, C.L. (2002). CCR4, a 3′-5′ poly(A) RNA and ssDNA exonuclease, is the catalytic component of the cytoplasmic deadenylase. EMBO J 21, 1414-1426.
Chen, Q., Adams, C.C., Usack, L., Yang, J., Monde, R.A., and Stern, D.B. (1995). An AU-rich element in the 3′ untranslated region of the spinach chloroplast petD gene participates in sequence-specific RNA-protein complex formation. Mol Cell Biol 15, 2010-2018.
Chou, W.L., Huang, L.F., Fang, J.C., Yeh, C.H., Hong, C.Y., Wu, S.J., and Lu, C.A. (2014). Divergence of the expression and subcellular localization of CCR4-associated factor 1 (CAF1) deadenylase proteins in Oryza sativa. Plant Mol Biol 85, 443-458.
Clark, L.B., Viswanathan, P., Quigley, G., Chiang, Y.C., McMahon, J.S., Yao, G., Chen, J., Nelsbach, A., and Denis, C.L. (2004). Systematic mutagenesis of the leucine-rich repeat (LRR) domain of CCR4 reveals specific sites for binding to CAF1 and a separate critical role for the LRR in CCR4 deadenylase activity. J Biol Chem 279, 13616-13623.
Collart, M.A., and Panasenko, O.O. (2012). The Ccr4--not complex. Gene 492, 42-53.
Collart, M.A., and Timmers, H.T. (2004). The eukaryotic Ccr4-not complex: a regulatory platform integrating mRNA metabolism with cellular signaling pathways? Prog Nucleic Acid Res Mol Biol 77, 289-322.
Cooke, A., Prigge, A., and Wickens, M. (2010). Translational repression by deadenylases. J Biol Chem 285, 28506-28513.
Cougot, N., Babajko, S., and Seraphin, B. (2004). Cytoplasmic foci are sites of mRNA decay in human cells. J Cell Biol 165, 31-40.
Dehlin, E., Wormington, M., Korner, C.G., and Wahle, E. (2000). Cap-dependent deadenylation of mRNA. EMBO J 19, 1079-1086.
Deluen, C., James, N., Maillet, L., Molinete, M., Theiler, G., Lemaire, M., Paquet, N., and Collart, M.A. (2002). The Ccr4-not complex and yTAF1 (yTaf(II)130p/yTaf(II)145p) show physical and functional interactions. Mol Cell Biol 22, 6735-6749.
Denis, C.L. (1984). Identification of new genes involved in the regulation of yeast alcohol dehydrogenase II. Genetics 108, 833-844.
Denis, C.L., Draper, M.P., Liu, H.Y., Malvar, T., Vallari, R.C., and Cook, W.J. (1994). The yeast CCR4 protein is neither regulated by nor associated with the SPT6 and SPT10 proteins and forms a functionally distinct complex from that of the SNF/SWI transcription factors. Genetics 138, 1005-1013.
Denis, C.L., and Malvar, T. (1990). The CCR4 gene from Saccharomyces cerevisiae is required for both nonfermentative and spt-mediated gene expression. Genetics 124, 283-291.
Dez, C., Houseley, J., and Tollervey, D. (2006). Surveillance of nuclear-restricted pre-ribosomes within a subnucleolar region of Saccharomyces cerevisiae. EMBO J 25, 1534-1546.
Dlakic, M. (2000). Functionally unrelated signalling proteins contain a fold similar to Mg2+-dependent endonucleases. Trends Biochem Sci 25, 272-273.
Doma, M.K., and Parker, R. (2007). RNA quality control in eukaryotes. Cell 131, 660-668.
Draper, M.P., Salvadore, C., and Denis, C.L. (1995). Identification of a mouse protein whose homolog in Saccharomyces cerevisiae is a component of the CCR4 transcriptional regulatory complex. Mol Cell Biol 15, 3487-3495.
Dupressoir, A., Morel, A.P., Barbot, W., Loireau, M.P., Corbo, L., and Heidmann, T. (2001). Identification of four families of yCCR4- and Mg2+-dependent endonuclease-related proteins in higher eukaryotes, and characterization of orthologs of yCCR4 with a conserved leucine-rich repeat essential for hCAF1/hPOP2 binding. BMC Genomics 2, 9.
Egecioglu, D.E., Henras, A.K., and Chanfreau, G.F. (2006). Contributions of Trf4p- and Trf5p-dependent polyadenylation to the processing and degradative functions of the yeast nuclear exosome. RNA 12, 26-32.
Eulalio, A., Behm-Ansmant, I., and Izaurralde, E. (2007). P bodies: at the crossroads of post-transcriptional pathways. Nat Rev Mol Cell Biol 8, 9-22.
Eystathioy, T., Chan, E.K., Tenenbaum, S.A., Keene, J.D., Griffith, K., and Fritzler, M.J. (2002). A phosphorylated cytoplasmic autoantigen, GW182, associates with a unique population of human mRNAs within novel cytoplasmic speckles. Mol Biol Cell 13, 1338-1351.
Fabian, M.R., Cieplak, M.K., Frank, F., Morita, M., Green, J., Srikumar, T., Nagar, B., Yamamoto, T., Raught, B., Duchaine, T.F., et al. (2011). miRNA-mediated deadenylation is orchestrated by GW182 through two conserved motifs that interact with CCR4-NOT. Nat Struct Mol Biol 18, 1211-1217.
Fang, F., Hoskins, J., and Butler, J.S. (2004). 5-fluorouracil enhances exosome-dependent accumulation of polyadenylated rRNAs. Mol Cell Biol 24, 10766-10776.
Gao, M., Fritz, D.T., Ford, L.P., and Wilusz, J. (2000). Interaction between a poly(A)-specific ribonuclease and the 5′ cap influences mRNA deadenylation rates in vitro. Mol Cell 5, 479-488.
Garneau, N.L., Wilusz, J., and Wilusz, C.J. (2007). The highways and byways of mRNA decay. Nat Rev Mol Cell Biol 8, 113-126.
Gay, N.J., Packman, L.C., Weldon, M.A., and Barna, J.C. (1991). A leucine-rich repeat peptide derived from the Drosophila Toll receptor forms extended filaments with a beta-sheet structure. FEBS Lett 291, 87-91.
Godwin, A.R., Kojima, S., Green, C.B., and Wilusz, J. (2013). Kiss your tail goodbye: the role of PARN, Nocturnin, and Angel deadenylases in mRNA biology. Biochim Biophys Acta 1829, 571-579.
Grigull, J., Mnaimneh, S., Pootoolal, J., Robinson, M.D., and Hughes, T.R. (2004). Genome-wide analysis of mRNA stability using transcription inhibitors and microarrays reveals posttranscriptional control of ribosome biogenesis factors. Mol Cell Biol 24, 5534-5547.
Gross, C.T., and McGinnis, W. (1996). DEAF-1, a novel protein that binds an essential region in a Deformed response element. EMBO J 15, 1961-1970.
Guo, W., Sun, B., Xiao, Z., Liu, Y., Wang, Y., Zhang, L., Wang, R., and Chen, S.R. (2016). The EF-hand Ca2+ Binding Domain Is Not Required for Cytosolic Ca2+ Activation of the Cardiac Ryanodine Receptor. J Biol Chem 291, 2150-2160.
Gutierrez, R.A., MacIntosh, G.C., and Green, P.J. (1999). Current perspectives on mRNA stability in plants: multiple levels and mechanisms of control. Trends Plant Sci 4, 429-438.
Havel, V.E., Wool, N.K., Ayad, D., Downey, K.M., Wilson, C.F., Larsen, P., Djordjevic, J.T., and Panepinto, J.C. (2011). Ccr4 promotes resolution of the endoplasmic reticulum stress response during host temperature adaptation in Cryptococcus neoformans. Eukaryot Cell 10, 895-901.
Herrick, D., Parker, R., and Jacobson, A. (1990). Identification and comparison of stable and unstable mRNAs in Saccharomyces cerevisiae. Mol Cell Biol 10, 2269-2284.
Ingelfinger, D., Arndt-Jovin, D.J., Luhrmann, R., and Achsel, T. (2002). The human LSm1-7 proteins colocalize with the mRNA-degrading enzymes Dcp1/2 and Xrnl in distinct cytoplasmic foci. RNA 8, 1489-1501.
Joly, W., Chartier, A., Rojas-Rios, P., Busseau, I., and Simonelig, M. (2013). The CCR4 deadenylase acts with Nanos and Pumilio in the fine-tuning of Mei-P26 expression to promote germline stem cell self-renewal. Stem Cell Reports 1, 411-424.
Kadaba, S., Krueger, A., Trice, T., Krecic, A.M., Hinnebusch, A.G., and Anderson, J. (2004). Nuclear surveillance and degradation of hypomodified initiator tRNAMet in S. cerevisiae. Genes Dev 18, 1227-1240.
Kedersha, N., Stoecklin, G., Ayodele, M., Yacono, P., Lykke-Andersen, J., Fritzler, M.J., Scheuner, D., Kaufman, R.J., Golan, D.E., and Anderson, P. (2005). Stress granules and processing bodies are dynamically linked sites of mRNP remodeling. J Cell Biol 169, 871-884.
Kedersha, N.L., Gupta, M., Li, W., Miller, I., and Anderson, P. (1999). RNA-binding proteins TIA-1 and TIAR link the phosphorylation of eIF-2 alpha to the assembly of mammalian stress granules. J Cell Biol 147, 1431-1442.
Kimball, S.R., Horetsky, R.L., Ron, D., Jefferson, L.S., and Harding, H.P. (2003). Mammalian stress granules represent sites of accumulation of stalled translation initiation complexes. Am J Physiol Cell Physiol 284, C273-284.
Kobe, B., and Kajava, A.V. (2001). The leucine-rich repeat as a protein recognition motif. Curr Opin Struct Biol 11, 725-732.
Korner, C.G., Wormington, M., Muckenthaler, M., Schneider, S., Dehlin, E., and Wahle, E. (1998). The deadenylating nuclease (DAN) is involved in poly(A) tail removal during the meiotic maturation of Xenopus oocytes. EMBO J 17, 5427-5437.
Kulkarni, M., Ozgur, S., and Stoecklin, G. (2010). On track with P-bodies. Biochem Soc Trans 38, 242-251.
LaCava, J., Houseley, J., Saveanu, C., Petfalski, E., Thompson, E., Jacquier, A., and Tollervey, D. (2005). RNA degradation by the exosome is promoted by a nuclear polyadenylation complex. Cell 121, 713-724.
Lau, N.C., Mulder, K.W., Brenkman, A.B., Mohammed, S., van den Broek, N.J., Heck, A.J., and Timmers, H.T. (2010). Phosphorylation of Not4p functions parallel to BUR2 to regulate resistance to cellular stresses in Saccharomyces cerevisiae. PLoS One 5, e9864.
Lenssen, E., Oberholzer, U., Labarre, J., De Virgilio, C., and Collart, M.A. (2002). Saccharomyces cerevisiae Ccr4-not complex contributes to the control of Msn2p-dependent transcription by the Ras/cAMP pathway. Mol Microbiol 43, 1023-1037.
Liu, H.Y., Chiang, Y.C., Pan, J., Chen, J., Salvadore, C., Audino, D.C., Badarinarayana, V., Palaniswamy, V., Anderson, B., and Denis, C.L. (2001). Characterization of CAF4 and CAF16 reveals a functional connection between the CCR4-NOT complex and a subset of SRB proteins of the RNA polymerase II holoenzyme. J Biol Chem 276, 7541-7548.
Liu, Y., Chen, W., Gaudet, J., Cheney, M.D., Roudaia, L., Cierpicki, T., Klet, R.C., Hartman, K., Laue, T.M., Speck, N.A., et al. (2007). Structural basis for recognition of SMRT/N-CoR by the MYND domain and its contribution to AML1/ETO′s activity. Cancer Cell 11, 483-497.
Lopez-Lastra, M., Rivas, A., and Barria, M.I. (2005). Protein synthesis in eukaryotes: the growing biological relevance of cap-independent translation initiation. Biol Res 38, 121-146.
Maillet, L., Tu, C., Hong, Y.K., Shuster, E.O., and Collart, M.A. (2000). The essential function of Not1 lies within the Ccr4-Not complex. J Mol Biol 303, 131-143.
Malvar, T., Biron, R.W., Kaback, D.B., and Denis, C.L. (1992). The CCR4 protein from Saccharomyces cerevisiae contains a leucine-rich repeat region which is required for its control of ADH2 gene expression. Genetics 132, 951-962.
Martinez, J., Ren, Y.G., Nilsson, P., Ehrenberg, M., and Virtanen, A. (2001). The mRNA cap structure stimulates rate of poly(A) removal and amplifies processivity of degradation. J Biol Chem 276, 27923-27929.
Matthews, J.M., Bhati, M., Lehtomaki, E., Mansfield, R.E., Cubeddu, L., and Mackay, J.P. (2009). It takes two to tango: the structure and function of LIM, RING, PHD and MYND domains. Curr Pharm Des 15, 3681-3696.
Mittal, S., Aslam, A., Doidge, R., Medica, R., and Winkler, G.S. (2011). The Ccr4a (CNOT6) and Ccr4b (CNOT6L) deadenylase subunits of the human Ccr4-Not complex contribute to the prevention of cell death and senescence. Mol Biol Cell 22, 748-758.
Morita, M., Suzuki, T., Nakamura, T., Yokoyama, K., Miyasaka, T., and Yamamoto, T. (2007). Depletion of mammalian CCR4b deadenylase triggers elevation of the p27Kip1 mRNA level and impairs cell growth. Mol Cell Biol 27, 4980-4990.
Morris, J.Z., Hong, A., Lilly, M.A., and Lehmann, R. (2005). twin, a CCR4 homolog, regulates cyclin poly(A) tail length to permit Drosophila oogenesis. Development 132, 1165-1174.
Muhlrad, D., and Parker, R. (2005). The yeast EDC1 mRNA undergoes deadenylation-independent decapping stimulated by Not2p, Not4p, and Not5p. EMBO J 24, 1033-1045.
Nakayama, S., and Kretsinger, R.H. (1994). Evolution of the EF-hand family of proteins. Annu Rev Biophys Biomol Struct 23, 473-507.
Nousch, M., Techritz, N., Hampel, D., Millonigg, S., and Eckmann, C.R. (2013). The Ccr4-Not deadenylase complex constitutes the main poly(A) removal activity in C. elegans. J Cell Sci 126, 4274-4285.
Opyrchal, M., Anderson, J.R., Sokoloski, K.J., Wilusz, C.J., and Wilusz, J. (2005). A cell-free mRNA stability assay reveals conservation of the enzymes and mechanisms of mRNA decay between mosquito and mammalian cell lines. Insect Biochem Mol Biol 35, 1321-1334.
Parker, R., and Song, H. (2004). The enzymes and control of eukaryotic mRNA turnover. Nat Struct Mol Biol 11, 121-127.
Sakai, A., Chibazakura, T., Shimizu, Y., and Hishinuma, F. (1992). Molecular analysis of POP2 gene, a gene required for glucose-derepression of gene expression in Saccharomyces cerevisiae. Nucleic Acids Res 20, 6227-6233.
Schoenberg, D.R. (2011). Mechanisms of endonuclease-mediated mRNA decay. Wiley Interdiscip Rev RNA 2, 582-600.
Schwede, A., Ellis, L., Luther, J., Carrington, M., Stoecklin, G., and Clayton, C. (2008). A role for Caf1 in mRNA deadenylation and decay in trypanosomes and human cells. Nucleic Acids Res 36, 3374-3388.
Shaw, G., and Kamen, R. (1986). A conserved AU sequence from the 3′ untranslated region of GM-CSF mRNA mediates selective mRNA degradation. Cell 46, 659-667.
Sheth, U., and Parker, R. (2003). Decapping and decay of messenger RNA occur in cytoplasmic processing bodies. Science 300, 805-808.
Shirai, Y.T., Suzuki, T., Morita, M., Takahashi, A., and Yamamoto, T. (2014). Multifunctional roles of the mammalian CCR4-NOT complex in physiological phenomena. Front Genet 5, 286.
Song, D., Li, L.S., Heaton-Johnson, K.J., Arsenault, P.R., Master, S.R., and Lee, F.S. (2013). Prolyl hydroxylase domain protein 2 (PHD2) binds a Pro-Xaa-Leu-Glu motif, linking it to the heat shock protein 90 pathway. J Biol Chem 288, 9662-9674.
Spadaccini, R., Perrin, H., Bottomley, M.J., Ansieau, S., and Sattler, M. (2006). Structure and functional analysis of the MYND domain. J Mol Biol 358, 498-508.
St Johnston, D. (2005). Moving messages: the intracellular localization of mRNAs. Nat Rev Mol Cell Biol 6, 363-375.
Struijs, P.A., Smidt, N., Arola, H., Dijk v, C., Buchbinder, R., and Assendelft, W.J. (2002). Orthotic devices for the treatment of tennis elbow. Cochrane Database Syst Rev, CD001821.
Suzuki, Y., Arae, T., Green, P.J., Yamaguchi, J., and Chiba, Y. (2015). AtCCR4a and AtCCR4b are Involved in Determining the Poly(A) Length of Granule-bound starch synthase 1 Transcript and Modulating Sucrose and Starch Metabolism in Arabidopsis thaliana. Plant Cell Physiol 56, 863-874.
Tamura, K., Peterson, D., Peterson, N., Stecher, G., Nei, M., and Kumar, S. (2011). MEGA5: molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods. Molecular biology and evolution 28, 2731-2739.
Temme, C., Zaessinger, S., Meyer, S., Simonelig, M., and Wahle, E. (2004). A complex containing the CCR4 and CAF1 proteins is involved in mRNA deadenylation in Drosophila. EMBO J 23, 2862-2871.
Temme, C., Zhang, L., Kremmer, E., Ihling, C., Chartier, A., Sinz, A., Simonelig, M., and Wahle, E. (2010). Subunits of the Drosophila CCR4-NOT complex and their roles in mRNA deadenylation. RNA 16, 1356-1370.
Tiedje, C., Kotlyarov, A., and Gaestel, M. (2010). Molecular mechanisms of phosphorylation-regulated TTP (tristetraprolin) action and screening for further TTP-interacting proteins. Biochem Soc Trans 38, 1632-1637.
Tucker, M., Staples, R.R., Valencia-Sanchez, M.A., Muhlrad, D., and Parker, R. (2002). Ccr4p is the catalytic subunit of a Ccr4p/Pop2p/Notp mRNA deadenylase complex in Saccharomyces cerevisiae. EMBO J 21, 1427-1436.
Tucker, M., Valencia-Sanchez, M.A., Staples, R.R., Chen, J., Denis, C.L., and Parker, R. (2001). The transcription factor associated Ccr4 and Caf1 proteins are components of the major cytoplasmic mRNA deadenylase in Saccharomyces cerevisiae. Cell 104, 377-386.
Viswanathan, P., Chen, J., Chiang, Y.C., and Denis, C.L. (2003). Identification of multiple RNA features that influence CCR4 deadenylation activity. J Biol Chem 278, 14949-14955.
Wagner, E., Clement, S.L., and Lykke-Andersen, J. (2007). An unconventional human Ccr4-Caf1 deadenylase complex in nuclear cajal bodies. Mol Cell Biol 27, 1686-1695.
Wang, H., Morita, M., Yang, X., Suzuki, T., Yang, W., Wang, J., Ito, K., Wang, Q., Zhao, C., Bartlam, M., et al. (2010). Crystal structure of the human CNOT6L nuclease domain reveals strict poly(A) substrate specificity. EMBO J 29, 2566-2576.
Weber, C., Nover, L., and Fauth, M. (2008). Plant stress granules and mRNA processing bodies are distinct from heat stress granules. Plant J 56, 517-530.
Wells, S.E., Hillner, P.E., Vale, R.D., and Sachs, A.B. (1998). Circularization of mRNA by eukaryotic translation initiation factors. Mol Cell 2, 135-140.
Wilczynska, A., Aigueperse, C., Kress, M., Dautry, F., and Weil, D. (2005). The translational regulator CPEB1 provides a link between dcp1 bodies and stress granules. J Cell Sci 118, 981-992.
Winkler, G.S., and Balacco, D.L. (2013). Heterogeneity and complexity within the nuclease module of the Ccr4-Not complex. Front Genet 4, 296.
Wyers, F., Rougemaille, M., Badis, G., Rousselle, J.C., Dufour, M.E., Boulay, J., Regnault, B., Devaux, F., Namane, A., Seraphin, B., et al. (2005). Cryptic pol II transcripts are degraded by a nuclear quality control pathway involving a new poly(A) polymerase. Cell 121, 725-737.
Xiong, H., Feng, X., Gao, L., Xu, L., Pasek, D.A., Seok, J.H., and Meissner, G. (1998). Identification of a two EF-hand Ca2+ binding domain in lobster skeletal muscle ryanodine receptor/Ca2+ release channel. Biochemistry 37, 4804-4814.
Yamashita, A., Chang, T.C., Yamashita, Y., Zhu, W., Zhong, Z., Chen, C.Y., and Shyu, A.B. (2005). Concerted action of poly(A) nucleases and decapping enzyme in mammalian mRNA turnover. Nat Struct Mol Biol 12, 1054-1063.
Zaessinger, S., Busseau, I., and Simonelig, M. (2006). Oskar allows nanos mRNA translation in Drosophila embryos by preventing its deadenylation by Smaug/CCR4. Development 133, 4573-4583.
Zheng, D., Ezzeddine, N., Chen, C.Y., Zhu, W., He, X., and Shyu, A.B. (2008). Deadenylation is prerequisite for P-body formation and mRNA decay in mammalian cells. J Cell Biol 182, 89-101.
指導教授 陸重安(Chung-An Lu) 審核日期 2016-7-26
推文 facebook   plurk   twitter   funp   google   live   udn   HD   myshare   reddit   netvibes   friend   youpush   delicious   baidu   
網路書籤 Google bookmarks   del.icio.us   hemidemi   myshare   

若有論文相關問題,請聯絡國立中央大學圖書館推廣服務組 TEL:(03)422-7151轉57407,或E-mail聯絡  - 隱私權政策聲明