滨海沙地大头典竹叶片响应盐胁迫差异蛋白的鉴定与分析

Identification and analysis of differential expression proteins in response to salt stress in the leaves of Bambusa beecheyana var.pubescens in coastal dunes

对大头典竹幼苗叶片盐胁迫前后的差异蛋白进行鉴定与分析,揭示盐胁迫对大头典竹的蛋白功能和代谢通路的影响.大头典竹2年生幼苗在0.4%、0.6%NaCl溶液浇灌7 d后,提取叶片蛋白进行双向凝胶电泳,并筛选差异显著的蛋白进行质谱鉴定.0.4%和0.6%NaCl溶液处理时,差异蛋白表达量变化显著,共鉴定出15个差异蛋白点.15个差异蛋白涉及生物过程、分子功能和细胞组分等方面,KEGG代谢通路参与了10条,以碳代谢作用、乙醛酸和二羧酸代谢为主.0.4%和0.6%NaCl处理的叶绿体PsbP、放氧增强子蛋白1、核酮糖-1,5-二磷酸羧化酶、谷氨酰胺合成酶、抗坏血酸过氧化物酶2、磷酸甘油酸激酶的蛋白表达量显著上调,ATP合酶β亚基蛋白表达量显著下调,而ATP合酶α亚基表达量呈现先上调后下调的趋势.差异蛋白对盐胁迫的响应反映了植物在蛋白功能表达和代谢途径上对逆境的协调和自适应.

In order to explore the adjustments of protein function and metabolic pathways of Bambusa beecheyana var.pubescens under salt stress in sandy coast,the differential proteins of B.beecheyana seedlings before and after salt stress were compared.After irrigating with 0.4%and 0.6%NaCl solutions for 7 d,the differential proteins in the leaves of biennial B.beecheyana seedlings were extracted for two-dimensional gel electrophoresis,and the proteins with significant differences were screened and identified by mass spectrometry.The results showed that expression levels of differential proteins varied significantly under 0.4%and 0.6%NaCl solutions.A total of 15 differential proteins were identified,whose roles ranging from biological processes,molecular functions to cell components.Ten KEGG metabolic pathways were identified,which involved in carbon metabolism,glyoxylate and dicarboxylate metabolism.Under both levels of stress,the expressions of oxygen-evolving enhancer protein 1,chloroplast PsbP proteins,ribulose 1,5-biphosphate carboxylase/oxygenase,phosphoglycerate kinase,glutamine synthetase and L-ascorbate peroxidase 2 were remarkablely up-regulated.The expression of ATP synthaseβsubunit was significantly down-regulated while the expression of subunitαstarted with a rise and then dropped.Together,the responses of differential proteins induced by salt stress reflects the adaptation of plant in respect of protein functional expression and metabolic pathway.