百合sHsp16.45的异源表达及功能分析
摘要
植物在遭受高温,低温或干旱等胁迫时,可产生热激蛋白(Hsp),其中分子量为12～42kD的被统称为小热激蛋白(sHsp)。这类蛋白在结构上的共同特点是具有保守的ACD结构域。热激蛋白做为分子伴侣,在逆境胁迫中可保护生物体内的功能性蛋白免遭不可逆转的变性,维持蛋白的正常折叠,促进已错误折叠和解聚的蛋白质恢复正确构象或引导其降解。植物小热激蛋白在抗逆境胁迫中的作用近几年已成为植物抗逆的一个重要研究方向。
本研究通过将百合小热激蛋白LimHsp16.45进行异源表达,发现该小热激蛋白能够有效提高大肠杆菌在受到高温或低温胁迫后的菌细胞活性,并在高温处理下检测到此蛋白的积累量增多。在拟南芥中,LimHsp16.45定位在内膜系统,不但可以响应热刺激,形成典型的热激颗粒(HSGs),还能提高拟南芥在高盐胁迫下的萌发率和对氧化胁迫的耐受。而且在高盐胁迫下,可观察到类HSGs的广泛存在,推测LimHsp16.45对于盐胁迫的响应可能也是通过形成寡聚体发挥生理功能的。
Suffering from the high temperature, low temperature or drought stress, the plant can produce heat shock protein (Hsp). The protein whose molecular weight is among12～42kD is called small heat shock protein (sHsp). Almost all kind of Hsp always has a conservative ACD domain on the structure. Heat shock protein, one kind of molecular chaperones in adversity stress, can protect the functional proteins from irreversible degeneration, maintain the folding structure of natural protein and promote the proteins that have already folded in wrong way or depolymerized from the right protein conformation to recovery or degradation. The role of small heat shock protein in plant has become one of the most important research directions in recent years.
Our research made use of Lily small heat shock protein-LimHsp16.45for heterologous expression. We found that LimHsp16.45can improve the cell activity of E.coli effectively under high or low temperature stress. And we also observed the accumulation of this sHsp increased after heat treatment. In Arabidopsis, LimHsp16.45is located on inner membrane system. It can not only respond the heat stimulus and form typical heat shock Granules (HSGs), but also improve seed germination ratio in high-salt-stress. LimHsp16.45can increase the tolerance against oxidative stress. We observed that HSGs also exist when seedlings of Arabidopsis grow in high-salt-stress. So we speculate that LimHsp16.45in salt stress response also play the physiological function by forming oligomers.
本研究通过将百合小热激蛋白LimHsp16.45进行异源表达,发现该小热激蛋白能够有效提高大肠杆菌在受到高温或低温胁迫后的菌细胞活性,并在高温处理下检测到此蛋白的积累量增多。在拟南芥中,LimHsp16.45定位在内膜系统,不但可以响应热刺激,形成典型的热激颗粒(HSGs),还能提高拟南芥在高盐胁迫下的萌发率和对氧化胁迫的耐受。而且在高盐胁迫下,可观察到类HSGs的广泛存在,推测LimHsp16.45对于盐胁迫的响应可能也是通过形成寡聚体发挥生理功能的。
Suffering from the high temperature, low temperature or drought stress, the plant can produce heat shock protein (Hsp). The protein whose molecular weight is among12～42kD is called small heat shock protein (sHsp). Almost all kind of Hsp always has a conservative ACD domain on the structure. Heat shock protein, one kind of molecular chaperones in adversity stress, can protect the functional proteins from irreversible degeneration, maintain the folding structure of natural protein and promote the proteins that have already folded in wrong way or depolymerized from the right protein conformation to recovery or degradation. The role of small heat shock protein in plant has become one of the most important research directions in recent years.
Our research made use of Lily small heat shock protein-LimHsp16.45for heterologous expression. We found that LimHsp16.45can improve the cell activity of E.coli effectively under high or low temperature stress. And we also observed the accumulation of this sHsp increased after heat treatment. In Arabidopsis, LimHsp16.45is located on inner membrane system. It can not only respond the heat stimulus and form typical heat shock Granules (HSGs), but also improve seed germination ratio in high-salt-stress. LimHsp16.45can increase the tolerance against oxidative stress. We observed that HSGs also exist when seedlings of Arabidopsis grow in high-salt-stress. So we speculate that LimHsp16.45in salt stress response also play the physiological function by forming oligomers.
引文
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[3]Cherian S., Reddy M.P., Ferreira R.B. (2006). Transgenic plants with improved dehydration-stress tolerance:progress and prospects, Biol.Plant.50:481-495.
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[5]朱玉贤,李毅.现代分子生物学(第2版).北京：高等教育出版社.7：281-283.
[6]Ritossn F. (1962). A new puffing pattern induced by temperature shock an.dDNP in Drosop-hila, Experientia.18:571-573.
[7]Tisseres A, Mitchell A K. (1974). Some new proteins induced by temperature shock in droso-phils, Mol.Boil.84:389-398.
[8]Milton J. Schlesinger. (1986). Heat Shock Proteins:The Search for Functions, The Journal of Cell Biology,103:321-325.
[9]Kelley PM, Schlesinger MJ. (1978). The effect of amino-acid analogues and heat shock on gene expression in chicken embryo fibroblasts, Cell.15:1277-1286.
[10]Lemaux PG, Herendeen SL, Bloch PL and Neidhardt FC. (1978). Transient rates of synthesis of individual polypeptides in E.coli following temperature shifts, Cell.13:427-434.
[11]Fink K and E Zeuther. (1978). Heat shock proteins in Tetrahymena. ICN-UCLA Symposium, Molecular Cell Biolology.12:103-115.
[12]Nover L, Scharf KD, Neumann D. (1983). Formation of cytoplasmic heat shock granules in tomato cell cultures and leaves, Molecular and Cellular Biology.3:1648-1655.
[13]Lin C.-Y., Roberts J.K., Key J.L. (1984). Acquisition of thermotolerance in soybean seedlings: synthesis and accumulation of heat shock proteins and their cellular localization, Plant Physiol.74:152-160.
[14]Vierling E. (1991). The role of heat shock proteins in plants, Annu. Rev. Plant Phys.42: 579-620.
[15]Horwitz J. (1992). Alpha-crystallin can function as a molecular chaperone, Proc Natl Acad Sci USA.89:10449-10453.
[16]Katiyar-Agarwal S, Agarwal M, Grover A. (2003). Heat-tolerant basmati rice engineered by over-expression of hsplOl, Plant Mol Biol.51:677-686.
[17]Yamada K., Fukao Y., Hayashi M., Fukazawa M., Suzuki I., Nishimura M. (2007). Cytosolic HSP90 Regulates the Heat Shock Response That Is Responsible for Heat Acclimation in Arabidopsis thaliana., J.Biol.Chem.282:37794-37804.
[18]Yuliang Zhou, Huhui Chen, Pu Chu, Yin Li, Bin Tan, Yu Ding, Edward W. T.Tsang, Liwen Jiang, Keqiang Wu, Shangzhi Huang. (2012). NnHSP17.5, a cytosolic class Ⅱ small heat shock protein gene from Nelumbo nucifera, contributes to seed germination vigor and seedling thermotolerance in transgenic Arabidopsis, Plant Cell Rep.31:379-389.
[19]Schlesinger M.J. (1990). Heat shock proteins, J.Biol.Chem.265:12111-12114.
[20]Schoffl F., Prandl R., Reindl A. (1998). Regulation of the heat shock response, Plant Physiol. 117:1135-1141.
[21]Kotak S., Larkindale J., Lee U., von Koskull-Doring P., Vierling E., Scharf K.D. (2007). Complexity of the heat stress response in plants, Curr. Opin. Plant Biol.10:310-316.
[22]Mohamed H., A1-Whaibi. (2010). Plant heat-shock proteins:A mini review, Journal of King Saud University.139-150.
[23]Barends T.R., Werbeck N.D., and Reinstein. (2010). Disaggregases in 4 dimensions, Curr. Opin. Struct. Biol.20:46-53.
[24]Martin A., Baker T.A., and Sauer R.T. (2005). Rebuilt AAA + motors reveal operating principles for ATP-fuelled machines, Nature.437:1115-1120.
[25]Schirmer E.C., Glover J.R., Singer M.A., and Lindquist S. (1996). HSP100/Clp proteins:a common mechanism explains diverse functions, Trends Biochem. Sci.21:289-296.
[26]Schrader E.K., Harstad K.G., and Matouschek A. (2009). Targeting proteins for degradation, Nat. Chem. Biol.5:815-822.
[27]Doyle S.M., Shorter J., Zolkiewski M., Hoskins J.R., Lindquist S., and Wickner S. (2007). Asymmetric deceleration of C1pB or Hsp104 ATPase activity unleashes protein-remodeling activity, Nat. Struct. Mol. Biol.14:114-122.
[28]Schaupp A., Marcinowski M., Grimminger V., Bosl B., and Walter S. (2007). Processing of proteins by the molecular chaperone Hsp104, J. Mol. Biol.370:674-686.
[29]Weber-Ban E.U., Reid B.G., Miranker A.D., and Horwich A.L. (1999). Global unfolding of a substrate protein by the Hsp100 chaperone C1pA, Nature.401:90-93.
[30]Goloubinoff P., Mogk A., Zvi A.P., Tomoyasu T., Bukau B. (1999). Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network, Proc. Natl. Acad. Sci. USA.96:13732-13737.
[31]Schirmer EC, Lindquist S, Vierling E. (1994). An Arabidopsis heat shock protein complements a thermotolerance defect in yeast, The Plant Cell.6:1899-1909.
[32]Welch W.J., and Feramisco J.R. (1982). Purification of the major mammalian heat shock proteins, J. Biol. Chem.257:14949-14959.
[33]Picard D. (2002). Heat-shock protein 90, a chaperone for folding and regulation, Cell. Mol. Life Sci.59:1640-1648.
[34]Pratt W.B., and Toft D.O. (2003). Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery, Exp. Biol. Med. (Maywood) 228:111-133.
[35]Smith D.F. (1998). Sequence motifs shared between chaperone components participating in the assembly of progesterone receptor complexes, Biol. Chem.379:283-288.
[36]Jakob U., Lilie H., Meyer I., and Buchner J. (1995). Transient interaction of Hsp90 with early unfolding intermediates of citrate synthase.Implications for heat shock in vivo, J. Biol. Chem.270:7288-7294.
[37]Pearl L.H., and Prodromou C. (2006). Structure and mechanism of the Hsp90 molecular chaperone machinery, Annu. Rev. Biochem.75:271-294.
[38]Taipale M., Jarosz D.F., and Lindquist S. (2010). HSP90 at the hub of protein homeostasis:emerging mechanistic insights, Nat. Rev. Mol. Cell Biol.11:515-528.
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