高山离子芥MAP激酶基因CbMAPK3的克隆及功能分析
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摘要
为了适应各种生物胁迫和非生物胁迫,植物在长期进化过程中形成了完整的调节机制,感受外界刺激,调整基因的表达,调节代谢途径。通过完整的信号调节系统,激活或者抑制适当的基因以响应外界刺激。由促分裂原活化蛋白激酶(MAPK)、促分裂原活化蛋白激酶激酶(MAPKK)、促分裂原活化蛋白激酶激酶激酶(MAPKKK)组成的磷酸化级联途径在酵母和动物细胞中,起着重要的信号传递作用。植物中,鉴定出了多种MAP激酶基因,大量的研究表明植物MAPK激酶可以被激素,非生物胁迫,病原体侵染所激活,也可以在细胞分裂的特定时期被激活。
高山离子芥是稀有的高山冰缘植物,具有较高的适应寒冷环境的能力。由于高山离子芥是一种胁迫耐受植物,我们克隆得到了高山离子芥中与抗逆境胁迫有关的MAP激酶基因CbMAPK3,并通过RT—PCR和Western blotting分析等方法研究了MAPK在高山离子芥抵御非生物胁迫过程中所发挥的作用。研究结果如下:
(1) 获得了高山离子芥MAP激酶基因CbMAPK3,全长1419bp,其中包括1110bp的开放阅读框(ORF),91bp的5′非翻译区(5′UTR),218bp的3′非翻译区(3′UTR),包括15bp的polyA。该基因编码一个369个氨基酸的蛋白质,分子量42.5kDa,等电点(PI)5.79。由于该基因与拟南芥AtMPK3同源性最高,达到了90%以上,因此命名为CbMAPK3(genbank accession number:AY805424)。CbMAPK3包含有MAP激酶所具有的11个保守序列区,以及MAP激酶的磷酸化位点TEY基序。因此该基因很可能编码一个MAP激酶蛋白。
(2) 序列分析结果显示,该蛋白与植物抗逆境胁迫有关的MAP激酶亚组A有很高的同源性,CbMAPK3与Arabidopsis AtMPK3同源性最高,达到了95%,其次是
Nicotiana tabacum NtWIPK(82%),Capsicum annuum CaMPKI(81%),PsMAPK3(80%),Medicago sativa MsMMK4(80%),Petrosecinum crispum PARSLEY MAPK(80%)。应用SOPMA在线分析将CbMAPK3预测蛋白序列进行二级结构预测,结果显示,CbMAPK3预测蛋白序列包含46%α—螺旋(alpha helix),13%伸展链
(extended strand),6%β—转角(beta turn),35%无规卷曲(random coil)。α—螺旋和无规卷曲为该蛋白的主要二级结构。
To survive biotic and abiotic stresses, plants have developed elaborate mechanisms to perceive external signals and adjust metabolic pathways by modulating the expression of genes. Activation and/ or inactivation of appropriate genes in response to particular stimuli are mediated through well-tuned signal transduction systems. The phosphorylation cascades including mitogen-activated protein kinases (MAPKs), MAPK kinases (MAPKKs), and MAPKK kinases (MAPKKKs) have been reported to function in various signal transduction pathways from yeasts to vertebrates. In plants, a variety of genes encoding MAPKs have been identified. Numerous studies shown that plant MAPK cascades are activated by hormones, abiotic stresses, pathogens and pathogen-derived elicitors, and also activated at specific stages during the cell cycle.Chorispora bungeana fisch. & C.A. Mey (Chorispora bungeana) is a rare alpine subnival plant species that is highly capable of resisting freezing environment. Since it is a Stress-tolerant plant, we have isolated from chorispora bungeana a new MAPK cDNA CbMAPK3 and investigated the participation of CbMAPK3 as possible mediators of abiotic stresses by RT-PCR and Western blotting. We got results as below:(1) Cloning and sequence analysis of the full-length cDNA of CbMAPK3. Based on cDNA sequences of the conserved regions of plant MAPK genes, we have isolated from chorispora bungeana a new MAPK cDNA CbMAPK3. The cloned full-length cDNA of CbMAPK3 was 1419bp with a polyA tail of 15bp. The cDNA contained a 1110bp ORF encoding a protein of 369 amino acids with a calculated molecular weight of about 42.5kDa and with a PI of 5.79. A 5' untranslated region (UTR) of 91bp was found upstream of the first ATG codon, and a 3' untranslated region (UTR) of 218bp was found downstream from the stop codon. The protein exhibit closest homology to a subgroup of plant MAPKs containing Arabidopsis AtMPK3 and we thus refer to them as CbMAPK3 (genbank accession number: AY805424). The CbMAPK3 protein contained all 11 conserved amino acid and peptide motifs characteristic of 11 subdomains of protein kinases with serin/threonine specificity. The TEY motif, which
includes the threonin and tyrosine residues whose phosphorylation is necessary for MAP kinase activation and is a characteristic feature of MAP kinase, is also conserved in the CbMAPK3 protein sequence.(2) Based on the phylogenetic tree of cloned plant MAPKs, CbMAPK3 can be grouped intosubgroup A. Comparison of the predicted protein sequences of the CbMAPK3 with MAP kinases of other plants shows that CbMAPK3 is most homologous to the Arabidopsis AtMPK3 (95%), Nicotiana tabacum NtWIPK (82%), Capsicum annuum CaMPKl (81%), PsMAPK3 (80%), Medicago saliva MsMMK4 (80%), Petrosecinum crispum PARSLEY MAPK (80%). The secondary structure of the putative CbMAPK3 protein was analyzed by SOPMA. The result showed that the putative CbMAPK3 peptide contained 46% alpha helix, 13% extended strand, 6% beta turn, and 35% random coil. The alpha helix and random coil constituted interlaced domination of the main part of the secondary structure. From the above sequence analyses, CbMAPK3 was found to have many characteristics common to the MAPKs in plant and family A members tend to share highly similar sequences.(3) Investigate CbMAPK3 expression pattern in various tissues of chorispora bungeana,the result shown that its expression has almost no tissue specificity.(4) CbMAPK3 expression patterns under cold and other abiotic stresses were analyzed bysemi-quantitative RT-PCR. After exposure to 4°C, transcript levels of CbMAPK3 increased rapidly, maximum levels was observed 0.5 h after cold treatment, then, the CbMAPK3 transcript declined gradually and fell to the basal level at 24 h. When chorispora bungeana was exposure to -4°C, transcript levels of CbMAPK3 also increased rapidly, but the transcript maintained at a high levels up to 24h. To our knowledge, this is the first description of a plant MAPK gene whose expression is inducible at -4°C treatment. The expression of CbMAPK3 could also be induced by salt stress and ABA treatment, under salt stress, the transcripts of CbMAPK3 increased to a high level after 2h and maintained high levels at 48h after treatment. When treated with ABA, the transcripts of CbMAPK3 increased significantly after 30*min, and decreased after 12h. indicating that the CbMAPK3 gene was ABA-dependent.
On the whole, the CbMAPK3 transcript levels were increased by cold (4°C and -4°C), salt and ABA treatment. The increase in expression of MAPK gene may contribute to the stress response by increasing the amount of proteins available for activation. Therefore, it can be concluded that MAPK not only become activated by posttranslational phosphorylation of the highly conserved threonine and tyrosine residue through upstream kinases, transcriptional control is also an important mechanism in MAPK signaling cascades in plant.(5) Investigate CbMAPK3 protein level under cold and other abiotic stresses. Immunoblot analysis using a -C-MPK3 antibody show that the protein level of CbMAPK3 was increased significantly and maximum levels was observed at 3h after 4°C cold treatment, then, the CbMAPK3 protein level declined gradually and fell to the basal level at 24 h . but the protein level of CbMAPK3 was increased slightly by 0°C cold treatment. When treat with 150mM NaCL, the protein level of CbMAPK3 increased after 3h and declined after 12h. The increase in protein level of MAPK may also contribute to the stress response by increasing the amount of proteins available for activation. Therefore, it can be concluded that protein level control is also an important mechanism in MAPK signaling cascades in plant.(6) To comfirm whether CbMAPK3 has the osmo-protection function, the coding regionwas subcloned into prokaryotic expression vector. E. coli (sri.TnlO) cell transformed with this plasmid exhibitad no significantly better growth in the presence of 1M sorbitol, compared to E. coli (srl::TnlO) transformed with the vector only, after induction with IPTG. we can conclude that CbMAPK3 is likely involved in abiotic stress responses as a signal transduction element, but itself did not has the function of osmo-protection.(7) Expression of CbMAPK3 in E. coli BL21. The coding region of CbMAPK3 cDNA wassubcloned into the bacterial expression vector pET30a, and transformed E. coli BL21. After induced by IPTG, the expression protein had a molecular mass of about 46kD by SDS-PAGE, corresponding to the deduced amino acid sequence of CbMAPK3 fusion protein. Western blotting analysis using a -C-MPK3 antibody showed that the BL21/ pET30a/CbMAPK3 samples had positive signal at 46kD position, where there is no
signal in BL21/ pET30a samples. This result confirmed that a -C-MPK3 antibody specifically reacted with CbMAPK3 protein. So, we can further conclude that the protein reacted with a -C-MPK3 antibody in the whole protein of Chorispora bungeana is CbMAPK3.In conclusion, a novel MAPK gene CbMAPK3 was identified and characterized. The expression of CbMAPK3 was induced by cold, salt, and ABA but no tissue specificity.The protein level of CbMAPK3 increased when treated with cold (4 and -4 °C) and salinity stress. These results indicate that the CbMAPK3 may play an important role in response to environmental stresses.
高山离子芥是稀有的高山冰缘植物,具有较高的适应寒冷环境的能力。由于高山离子芥是一种胁迫耐受植物,我们克隆得到了高山离子芥中与抗逆境胁迫有关的MAP激酶基因CbMAPK3,并通过RT—PCR和Western blotting分析等方法研究了MAPK在高山离子芥抵御非生物胁迫过程中所发挥的作用。研究结果如下:
(1) 获得了高山离子芥MAP激酶基因CbMAPK3,全长1419bp,其中包括1110bp的开放阅读框(ORF),91bp的5′非翻译区(5′UTR),218bp的3′非翻译区(3′UTR),包括15bp的polyA。该基因编码一个369个氨基酸的蛋白质,分子量42.5kDa,等电点(PI)5.79。由于该基因与拟南芥AtMPK3同源性最高,达到了90%以上,因此命名为CbMAPK3(genbank accession number:AY805424)。CbMAPK3包含有MAP激酶所具有的11个保守序列区,以及MAP激酶的磷酸化位点TEY基序。因此该基因很可能编码一个MAP激酶蛋白。
(2) 序列分析结果显示,该蛋白与植物抗逆境胁迫有关的MAP激酶亚组A有很高的同源性,CbMAPK3与Arabidopsis AtMPK3同源性最高,达到了95%,其次是
Nicotiana tabacum NtWIPK(82%),Capsicum annuum CaMPKI(81%),PsMAPK3(80%),Medicago sativa MsMMK4(80%),Petrosecinum crispum PARSLEY MAPK(80%)。应用SOPMA在线分析将CbMAPK3预测蛋白序列进行二级结构预测,结果显示,CbMAPK3预测蛋白序列包含46%α—螺旋(alpha helix),13%伸展链
(extended strand),6%β—转角(beta turn),35%无规卷曲(random coil)。α—螺旋和无规卷曲为该蛋白的主要二级结构。
To survive biotic and abiotic stresses, plants have developed elaborate mechanisms to perceive external signals and adjust metabolic pathways by modulating the expression of genes. Activation and/ or inactivation of appropriate genes in response to particular stimuli are mediated through well-tuned signal transduction systems. The phosphorylation cascades including mitogen-activated protein kinases (MAPKs), MAPK kinases (MAPKKs), and MAPKK kinases (MAPKKKs) have been reported to function in various signal transduction pathways from yeasts to vertebrates. In plants, a variety of genes encoding MAPKs have been identified. Numerous studies shown that plant MAPK cascades are activated by hormones, abiotic stresses, pathogens and pathogen-derived elicitors, and also activated at specific stages during the cell cycle.Chorispora bungeana fisch. & C.A. Mey (Chorispora bungeana) is a rare alpine subnival plant species that is highly capable of resisting freezing environment. Since it is a Stress-tolerant plant, we have isolated from chorispora bungeana a new MAPK cDNA CbMAPK3 and investigated the participation of CbMAPK3 as possible mediators of abiotic stresses by RT-PCR and Western blotting. We got results as below:(1) Cloning and sequence analysis of the full-length cDNA of CbMAPK3. Based on cDNA sequences of the conserved regions of plant MAPK genes, we have isolated from chorispora bungeana a new MAPK cDNA CbMAPK3. The cloned full-length cDNA of CbMAPK3 was 1419bp with a polyA tail of 15bp. The cDNA contained a 1110bp ORF encoding a protein of 369 amino acids with a calculated molecular weight of about 42.5kDa and with a PI of 5.79. A 5' untranslated region (UTR) of 91bp was found upstream of the first ATG codon, and a 3' untranslated region (UTR) of 218bp was found downstream from the stop codon. The protein exhibit closest homology to a subgroup of plant MAPKs containing Arabidopsis AtMPK3 and we thus refer to them as CbMAPK3 (genbank accession number: AY805424). The CbMAPK3 protein contained all 11 conserved amino acid and peptide motifs characteristic of 11 subdomains of protein kinases with serin/threonine specificity. The TEY motif, which
includes the threonin and tyrosine residues whose phosphorylation is necessary for MAP kinase activation and is a characteristic feature of MAP kinase, is also conserved in the CbMAPK3 protein sequence.(2) Based on the phylogenetic tree of cloned plant MAPKs, CbMAPK3 can be grouped intosubgroup A. Comparison of the predicted protein sequences of the CbMAPK3 with MAP kinases of other plants shows that CbMAPK3 is most homologous to the Arabidopsis AtMPK3 (95%), Nicotiana tabacum NtWIPK (82%), Capsicum annuum CaMPKl (81%), PsMAPK3 (80%), Medicago saliva MsMMK4 (80%), Petrosecinum crispum PARSLEY MAPK (80%). The secondary structure of the putative CbMAPK3 protein was analyzed by SOPMA. The result showed that the putative CbMAPK3 peptide contained 46% alpha helix, 13% extended strand, 6% beta turn, and 35% random coil. The alpha helix and random coil constituted interlaced domination of the main part of the secondary structure. From the above sequence analyses, CbMAPK3 was found to have many characteristics common to the MAPKs in plant and family A members tend to share highly similar sequences.(3) Investigate CbMAPK3 expression pattern in various tissues of chorispora bungeana,the result shown that its expression has almost no tissue specificity.(4) CbMAPK3 expression patterns under cold and other abiotic stresses were analyzed bysemi-quantitative RT-PCR. After exposure to 4°C, transcript levels of CbMAPK3 increased rapidly, maximum levels was observed 0.5 h after cold treatment, then, the CbMAPK3 transcript declined gradually and fell to the basal level at 24 h. When chorispora bungeana was exposure to -4°C, transcript levels of CbMAPK3 also increased rapidly, but the transcript maintained at a high levels up to 24h. To our knowledge, this is the first description of a plant MAPK gene whose expression is inducible at -4°C treatment. The expression of CbMAPK3 could also be induced by salt stress and ABA treatment, under salt stress, the transcripts of CbMAPK3 increased to a high level after 2h and maintained high levels at 48h after treatment. When treated with ABA, the transcripts of CbMAPK3 increased significantly after 30*min, and decreased after 12h. indicating that the CbMAPK3 gene was ABA-dependent.
On the whole, the CbMAPK3 transcript levels were increased by cold (4°C and -4°C), salt and ABA treatment. The increase in expression of MAPK gene may contribute to the stress response by increasing the amount of proteins available for activation. Therefore, it can be concluded that MAPK not only become activated by posttranslational phosphorylation of the highly conserved threonine and tyrosine residue through upstream kinases, transcriptional control is also an important mechanism in MAPK signaling cascades in plant.(5) Investigate CbMAPK3 protein level under cold and other abiotic stresses. Immunoblot analysis using a -C-MPK3 antibody show that the protein level of CbMAPK3 was increased significantly and maximum levels was observed at 3h after 4°C cold treatment, then, the CbMAPK3 protein level declined gradually and fell to the basal level at 24 h . but the protein level of CbMAPK3 was increased slightly by 0°C cold treatment. When treat with 150mM NaCL, the protein level of CbMAPK3 increased after 3h and declined after 12h. The increase in protein level of MAPK may also contribute to the stress response by increasing the amount of proteins available for activation. Therefore, it can be concluded that protein level control is also an important mechanism in MAPK signaling cascades in plant.(6) To comfirm whether CbMAPK3 has the osmo-protection function, the coding regionwas subcloned into prokaryotic expression vector. E. coli (sri.TnlO) cell transformed with this plasmid exhibitad no significantly better growth in the presence of 1M sorbitol, compared to E. coli (srl::TnlO) transformed with the vector only, after induction with IPTG. we can conclude that CbMAPK3 is likely involved in abiotic stress responses as a signal transduction element, but itself did not has the function of osmo-protection.(7) Expression of CbMAPK3 in E. coli BL21. The coding region of CbMAPK3 cDNA wassubcloned into the bacterial expression vector pET30a, and transformed E. coli BL21. After induced by IPTG, the expression protein had a molecular mass of about 46kD by SDS-PAGE, corresponding to the deduced amino acid sequence of CbMAPK3 fusion protein. Western blotting analysis using a -C-MPK3 antibody showed that the BL21/ pET30a/CbMAPK3 samples had positive signal at 46kD position, where there is no
signal in BL21/ pET30a samples. This result confirmed that a -C-MPK3 antibody specifically reacted with CbMAPK3 protein. So, we can further conclude that the protein reacted with a -C-MPK3 antibody in the whole protein of Chorispora bungeana is CbMAPK3.In conclusion, a novel MAPK gene CbMAPK3 was identified and characterized. The expression of CbMAPK3 was induced by cold, salt, and ABA but no tissue specificity.The protein level of CbMAPK3 increased when treated with cold (4 and -4 °C) and salinity stress. These results indicate that the CbMAPK3 may play an important role in response to environmental stresses.
引文
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