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標題: 利用二維電泳分析綠竹筍 Bambusa oldhamii與冬筍 Phyllostachys edulis 粒線體的蛋白質
Analysis of mitochondrial proteins in bamboo Bambusa oldhamii and Phyllostachys edulis by two-dimensional polyacrylamide gel electrophoresis
作者: 柯冠仲
Ko, Guang-Chung
關鍵字: bamboo
出版社: 生命科學系所
引用: Ahsan, N., Lee, D.G., Lee, S.H., Kang, K.Y., Bahk, J.D., Choi, M.S., Lee, I.J., Renaut, J. and Lee, B.H. (2007) A comparative proteomic analysis of tomato leaves in response to waterlogging stress. Physiol. Plant. 131, 555-570. Baginsky, S. and Gruissem, W. (2006) Arabidopsis thaliana proteomics: from proteome to genome. J. Exp. Bot. 57, 1485-1491. Boekema, E.J. and Braun, H.P. (2007) Supramolecular structure of the mitochondrial oxidative phosphorylation system. J. Biol. Chem. 282, 1-4 Brookes, P.S., Pinner, A., Ramachandran, A., Coward, L., Barnes, S., Kim, H. and Darley-Usmar, V.M. (2002) High throughput two-dimensional blue-native electrophoresis: a tool for functional proteomics of mitochondria and signaling complexes. Proteomics, 2, 969-977. Catusse J., Strub J.M., Job C., van Dorsselaer A. and Job, D. (2008) Proteome-wide characterization of sugarbeet seed vigor and its tissue specific expression. Proc. Natl. Acad. Sci. U S A. 105, 10262-10267. Cardol, P., González-Halphen, D., Reyes-Prieto, A., Baurain, D., Matagne, R.F. and Remacle, C. (2005) The mitochondrial oxidative phosphorylation proteome of Chlamydomonas reinhardtii deduced from the genome sequencing project. Plant Physiol. 137, 447-459. Deytieux, C., Geny, L., Lapaillerie, D., Claverol, S., Bonneu, M. and Donèche, B. (2007) Proteome analysis of grape skins during ripening. J. Exp. Bot. 58, 1851-1862. Dudkina, N.V., Eubel, H., Keegstra, W., Bokema, E.J. and Braun, H.P. (2005) Structure of a mitochondria supercomplex formed by respiratory chain Complexes I and III. Proc. Natl. Acad. Sci. U S A. 102, 3225-3229 Dudkina, N.V. Heinemeyer, J. Sunderhaus, S. Boekema, E.J. and Braun, H.P. (2006) Respiratory chain supercomplexes in the plant mitochondrial membrane. Trends Plant Sci. 11, 232-240. Eubel, H., Braun, H.P. and Millar, A.H. (2005) Blue-native PAGE in plants: a tool in analysis of protein-protein interactions. Plant Methods, 1, 11-23. Eubel, H., Heinemeyer, J. and Braun, H.P. (2004a) Identification and characterization of respirasomes in potato mitochondria. Plant Physiol. 134, 1450-1459. Eubel, H., Heinemeyer, J., Sunderhaus, S. and Braun, H.P. (2004b) Respiratory chain supercomplexes in plant mitochondria. Plant Physiol. Biochem. 42, 937-942. Eubel, H., Jänsch, L. and Braun, H.P. (2003) New insights into the respiratory chain of plant mitochondria. Supercomplexes and a unique composition of complex II. Plant Physiol. 133, 274-286. Grandier-Vazeille, X. and Guérin, M. (1996) Separation by blue native and colorless native polyacylamide gel electrophoresis of the oxidative phosphorylation complexes of yeast mitochondria solubilized by different detergents: specific staining of the different complexes. Anal. Biochem. 242, 248-254 Heazlewood, J.L., Howell, K.A., Whelan, J. and Millar, A.H. (2003a) Towards an analysis of the rice mitochondrial proteome. Plant Physiol. 132, 230-242. Heazlewood, J.L., Whelan, J. and Millar, A.H. (2003b) The products of the mitochondrial orf25 and orfB genes are FO components in the plant F1FO ATP synthase. FEBS. Lett. 540, 201-205. Hoa, L.T.P., Nomura, M., Kajiwara, H., Day, D.A. and Tajima, S. (2004) Proteomic analysis on symbiotic differentiation of mitochondria in soybean nodules. Plant Cell Physiol. 45, 300-308. Jänsch, L., Kruft, V., Schmitz, U.K. and Braun, H.P. (1996) New insights into the composition, molecular mass and stoichiometry of the protein complexes of plant mitochondria. Plant J. 9, 357-368. Kesseler, A., Diolez, P., Brinkmann, K. and Brand, M.D. (1992) Characterisation of the control of respiration in potato tuber mitochondria using the top-down approach of metabolic control analysis. Eur. J. Biochem. 210, 775-784. Khalsa-Moyers, G. and McDonald, W.H. (2006) Developments in mass spectrometry for the analysis of complex protein mixtures. Brief. Funct. Genomic. Proteomic. 5, 98-111. Khoudoli, G.A., Poter, I.M., Blow, J.J. and Swedlow, J.R. (2004) Optimisation of the two-dimensional gel electrophoresis protocol using the Taguchi approach. Proteome Science, 2:6. Komatsu, S., Konishi, H. and Hashimoto, M. (2007) The proteomics of plant cell membranes. J. Exp. Bot. 58, 103-112. Krause, F., Reifschneider, N.H., Vocke, D., Seelert, H., Rexroth, S. and Dencher, N.A. (2004a) “Respirasome”-like supercomplexes in green leaf mitochondria of spinach. J. Biol. Chem. 279, 48369-48375. Krause, F., Scheckhuber, C.Q., Werner, A., Rexroth, S., Reifschneider, N.H., Dencher, N.A. and Osiewacz, H.D. (2004b) Supramolecular organization of cytochrome c oxidase- and alternative oxidase-dependent respiratory chains in the filamentous fungus Podospora anserine. J. Biol. Chem. 279, 26453-26461. Kruft, V., Eubel, H., Jänsch, L., Werhahn, W. and Braun, H.P. (2001) Proteomic approach to identify novel mitochondrial proteins in Arabidopsis. Plant Physiol. 127, 1694-1710. Lee, K., Lee, J., Kim, Y., Bae, D., Kang, K.Y., Yoon, S.C. and Lim, D. (2004) Defining the plant disulfide proteome. Electrophoresis, 25, 532-541. Lenaz, G. and Genova, M.L. (2007) Kinetics of integrated electron transfer in the mitochondrial respiratory chain: random collision vs. solid state electron channeling. Am J. Physiol Cell Physiol. 292, C1221-C1239. Li, J., Ogasawara, A., Odake, T., Umemura, T. and Tsunoda, K. (2004) A new isoelectric focusing system for fast two-dimensional gel electrophoresis using a low-concentration polyacrylamide gel supported by a loose multifilament string. Anal. Sci. 20, 1673-1679. Lilley, K.S. and Dupree, P. (2006) Methods of quantitative proteomics and their application to plant organelle characterization. J. Exp. Bot. 57, 1493-1499. Logan, D.C. (2006) The mitochondria compartment. J. Exp. Bot. 57, 1225-1243. Martins de Souza, D., Oliveira, B.M., Castro-Dias, E., Winck, F.V., Horiuchi, R.S., Baldasso, P.A., Caetano, H.T., Pires, N.K., Marangoni, S. and Novello, J.C. (2008) The untiring search for the most complete proteome representation: reviewing the methods. Brief. Funct. Genomic. Proreomic. 7, 312-321. McKenzie, M., Lazarou, M., Thorburn, D.R. and Ryan, M.T. (2007) Analysis of mitochondrial subunit assembly into respiratory chain complexes using blue native polyacrylamide gel electrophoresis. Anal. Biochem. 364, 128-137. Millar, A.H., Heazlewood, J.L., Kristensen, B.K., Braun, H.P. and Møller, L.M. (2005) The plant mitochondrial proteome. Trends Plant Sci. 10, 36-43. Millar, A.H., Sweetlove, L.J., Giegé, P. and Leaver, C.J. (2001) Analysis of the Arabidopsis mitochondrial proteome. Plant Physiol. 127, 1711-1727. Møller, I.M. and Gardeström, P. (2007) Plant mitochondria-more active than ever! Physiol. Plant. 129, 1-5. Navet, R., Jarmuszkiewicz, W., Douette, P., Sluse-Goffart, C.M. and Sluse, F.E. (2004) Mitochondrial respiratory chain complex patterns from Acanthamoeba castellanii and Lycopersicon esculentum: comparative analysis by BN-PAGE and evidence of protein-protein interaction between alternative oxidase and complex III. J. Bioenerg. Biomembr. 36, 471-479. Nevishskii, A.I., Vitek, O. and Aebersold, R. (2007) Analysis and validation of proteomic data generated by tandem mass spectrometry. Nat. Methods, 4, 787-797. Oh-Ishi, M. and Maeda, T. (2002) Separation techniques for high-molecular-mass proteins. J. Chromtogr. B. 771, 49-66. Peters, K., Dudkina, N.V., Jänsch, L., Braun, H.P. and Boekema, E.J. (2008) A structural investigation of complex I and I+III2 supercomplex from Zea mays at 11-13 Å resolution: assignment of the carbonic anhydrase domain and evidence for structural heterogeneity within complex I. (2008) Biochim. Biophys. Acta, 1777, 84-93. Perales, M., Eubel, H., Heinemeyer, J., Colaneri, A., Zabaleta, E. and Braun, H.P. (2005) Disruption of a nuclear gene encoding a mitochondrial gamma carbonic anhydrase reduces complex I and Supercomplex I+III2 Levels and alters mitochondrial physiology in Arabidopsis. J. Mol. Biol. 350, 263-277. Plummer, D.T. (1980) Assay methods. In An Introduction to Practical Biochemistry, 2nd edn. (Plummer, D.T., eds). British Library, pp. 119-159. Sabar, M., Balk, J. and Leaver, C.J. (2005) Histochemical staining and quantification of plant mitochondrial respiratory chain complexes using blue-native polyacrylamide gel electrophoresis. Plant J. 44, 893-901. Saddar, S., Dienhart, M.K. and Stuart, R.A. (2008) The F1F0-ATP synthase complex influences the assembly state of the cytochrome bc1-cytochrome oxidase supercomplex and its association with the TIM23 machinery. J. Biol. Chem. 283, 6677-6686. Schägger, H. (2001) Blue-native gels to isolate protein complexes from mitochondria. Methods Cell Biol. 65, 231-244. Schägger, H., Cramer, W.A. and von Jagow, G. (1994) Analysis of molecular masses and oligomeric states of protein complexes by blue native electrophoresis and isolation of membrane protein complexes by two-dimensional native electrophoresis. Anal. Biochem. 217, 220-230. Schägger, H., de Coo, R., Bauer, M.F., Hofmann, S., Godinot, C. and Brandt, U. (2004) Significance of respirasomes for the assembly/stability of human respiratory chain complex I. J. Biol. Chem. 279, 36349-36353. Schägger, H. and Pfeiffer, K. (2000) Supercomplexes in the respiratory chains of yeast and mammalian mitochondria. EMBO J. 19, 1777-1783. Schägger, H. and von Jagow, G. (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166, 368-379. Schägger, H. and von Jagow, G. (1991) Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form. Anal. Biochem. 199, 233-231. Stead, D.A., Paton, N.W., Missier, P., Embury, S.M., Hedeler, C., Jin, B., Brown, A.J. and Preece, A. (2008) Information quality in proteomics. Brief. Bioinform. 9, 174-188. Taiz, L. and Zeiger, E. (2002) Respiration and lipid metabolism. In Plant Physiology, 3rd ed. (Taiz, L. and Zeiger, E., eds). Massachusetts: Sinauer Associates, Inc. pp. 223-258. Taylor, N.L., Heazlewood, J.L., Day, D.A. and Millar, A.H. (2005) Differential impact of environmental stresses on the pea mitochondrial proteome. Mol. Cell Proteomics, 4, 1122-1133. van Lis, R., Atteia, A., Mendoza-Hernández, G. and González-Halphen, D. (2003) Identification of novel mitochondrial protein components of Chlamydomonas reinhardtii. A proteomic approach. Plant Physiol. 132, 318-330. van Lis, R., Atteia, A., Mendoza-Hernández, G., Groth, G., and Atteia, A. (2007) New insights into the unique structure of the F0F1-ATP synthase from the chlamdomonad algae Polytomella sp. and Chlamydomonas reinhardtii. Plant Physiol. 144, 1190-1199. Wang, M., You, J., Bemis, K.G., Tegeler, T.J. and Brown, D.P. (2008) Label-free mass spectrometry-based protein quantification technologies in proteomic analysis. Brief. Funct. Genomic. Proteomic.7, 329-339. Whitford, D. (2005) Protein expression, purification and characterization. In Proteins: Structure and Function (Whitford, D., eds). England: Wiley, pp. 313-346. Wittig, I. and Schägger, H. (2005) Advantages and limitations of clear-native PAGE. Proteomics, 5, 4338-4346. Wu, Y.C. (2006) Comparative analysis of mitochondrial supercomplexes from summer bamboo Bambusa oldhamii and winter bamboo Phyllostachys edulis by BN-PAGE. Master thesis of the Department of Life Science, National ChungChing University, Taiwan. Yoshimura, K., Masuda, A., Kuwano, M., Yokota, A. and Akashi, K. (2008) Programmed proteome response for drought avoidance/tolerance in the root of a C3 Xerophyte (wild watermelon) under water deficits. Plant Cell Physiol. 49, 226-241. Zerbetto, E., Vergani, L. and Dabbeni-Sala, F. (1997) Quantification of muscle mitochondrial oxidative phosphorylation enzymes via histochemical staining of blue native polyacrylamide gels. Electrophoresis, 18, 2059-2064.
摘要: 竹子是亞洲重要的經濟作物之一,其新生的幼芽生長非常快速,雖然機制還不清楚,但推測需要很大的能量去支持其快速的生長。為了瞭解竹筍能量的代謝,利用兩種二維膠體電泳 BN/SDS-PAGE 與IEF/SDS-PAGE來研究綠竹筍與冬筍的蛋白質組成。 BN/SDS-PAGE能夠將綠竹筍與冬筍粒線體的複合體V的7個次單元與複合體III的5個次單元分離,綠竹筍的8個次單元被挑選進行質譜LC-MS/MS 鑑定。其中6個蛋白質點被鑑定為ATP合成酶的組成次單元,包括屬於ATP合成酶α、β、γ、δ、b與d次單元,另外2個為複合體III 的α 與β次單元。 另一方面,利用IEF/SDS-PAGE分離綠竹筍與冬筍粒線體蛋白質,並得到數量眾多的蛋白質點,但兩種竹筍的蛋白質點分布情形卻明顯的不同。在冬筍中發現IEF/SDS-PAGE分離得到的高分子量(>50kD)蛋白質點較綠竹筍多,相反地,綠竹筍經IEF/SDS-PAGE分離得到的低分子量(<20 kD)的蛋白質點較冬筍多。經由MADI-TOF MS或LC-MS/MS分析,冬筍的21個蛋白質點被鑑定出身分。這些被鑑定的蛋白質可依功能分為四個群組。第一個群組是參與電子傳遞鏈的組成,包括ATP合成酶β次單元與複合體I 的J次單元。第二個群組是參與碳的代謝,包括兩個lipoamide dehydrogenases、兩個aconitate hydratases 與 Succinyl-CoA 合成酶β次單元。第三個群組是參與保護機制,包括五個HSPs、兩個binding protein homologues、兩個disulfide isomerases、兩個Mn-SODs與一個抗病相關的蛋白質。.第四個群組是參與各種各樣的代謝反應,包括一個ATP-dependent RNA helicase。
Bamboo is one of the important cash crops in Asia and its new shoot grows very rapidly. It was supposed that the rapid growth requires a huge amount of energy supplement and may relate to the mitochondrial energy metabolism. Therefore, the mitochondria isolated from young bamboo shoots of B. oldhamii and P. edulis were analyzed by 2D BN/SDS-PAGE and IEF/SDS-PAGE. There were seven subunits of F1F0-ATP synthase (complex V) and five subunits of ubiquinol-cytochrome c oxidoreductase (complex III) of both bamboo mitochondria were resolved on BN/SDS-PAGE. Eight protein spots in B. oldhamii were subjected to MS-based analysis, while six subunits were identified as α, β, γ, δ, b, and d subunits which constitute complex V, and two subunits as α and β subunits which constitute complex III. Mitochondrial proteins from B. oldhamii and P. edulis were separated and visualized on IEF/SDS-PAGE. In P. edulis, more spots with high molecular masses (>50 kD) were revealed on IEF/SDS-PAGE than those in B. oldhamii; on the contrary, in B. oldhamii, more spots with low molecular masses (<20 kD) were revealed than those in P. edulis. Twenty-one spots of P. edulis mitochondrial protein on IEF/SDS-PAGE were identified by MALDI-TOF MS or LC-MS/MS. These newly identified protein spots can be divided into four function groups. The first group represented major function of electron transport chain including the ATP synthase β subunit and the putative J subunit of complex I. The second group consisted of proteins participating in carbon metabolism including two lipoamide dehydrogenases, two aconitate hydratases and a Succinyl-CoA synthase beta subunit. The third group consisted of proteins involved in protection including five members of HSPs, two binding protein homologues, two disulfide isomerases, two Mn-SODs and a disease resistance-related protein. The forth group included proteins involving in various metabolisms including ATP-dependent RNA helicase.
其他識別: U0005-1002200916251500
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