Plant leaves respond to day/night cycling in a number of physiological ways. At the mRNA level, the expression of some genes changes during the 24 h period. To determine which proteins exhibited a rhythmic pattern of ...Plant leaves respond to day/night cycling in a number of physiological ways. At the mRNA level, the expression of some genes changes during the 24 h period. To determine which proteins exhibited a rhythmic pattern of expression, proteomic profiles in maize seedling leaves were analyzed by high-throughput two-dimensional gel electrophoresis, combined with MALDI-TOF MS technology. Of the 464 proteins that were detected with silver staining in a pH range of 4-7, 17 （3.66%） showed clock rhythmicity in their abundance. These proteins belonged to diverse functional groups and proteins involved in photosynthesis and carbon metabolism were over-represented. These findings provide a new perspective on the relationship between the physiological functions of leaves and the clock rhythmic system.展开更多
De-etiolation consists of a series of developmental and physiological changes that a plant undergoes in response to light.During this process light,an important environmental signal,triggers the inhibition of mesocoty...De-etiolation consists of a series of developmental and physiological changes that a plant undergoes in response to light.During this process light,an important environmental signal,triggers the inhibition of mesocotyl elongation and the production of photosynthetically active chloroplasts,and etiolated leaves transition from the"sink"stage to the"source"stage.De-etiolation has been extensively studied in maize(Zea mays L.).However,little is known about how this transition is regulated.In this study,we described a quantitative proteomic and phosphoproteomic atlas of the de-etiolation process in maize.We identified 16,420 proteins in proteome,among which 14,168 proteins were quantified.In addition,8746 phosphorylation sites within 3110 proteins were identified.From the combined proteomic and phosphoproteomic data,we identified a total of 17,436 proteins.Only 7.0%(998/14,168)of proteins significantly changed in abundance during de-etiolation.In contrast,26.6%of phosphorylated proteins exhibited significant changes in phosphorylation level;these included proteins involved in gene expression and homeostatic pathways and rate-limiting enzymes involved in photosynthetic light and carbon reactions.Based on phosphoproteomic analysis,34.0%(1057/3110)of phosphorylated proteins identified in this study contained more than 2 phosphorylation sites,and 37 proteins contained more than 16 phosphorylation sites,indicating that multi-phosphorylation is ubiquitous during the de-etiolation process.Our results suggest that plants might preferentially regulate the level of posttranslational modifications(PTMs)rather than protein abundance for adapting to changing environments.The study of PTMs could thus better reveal the regulation of de-etiolation.展开更多
基金supported by the National Basic Research Program of China(2007CB109000)the National Science Found for Distinguished Young Scholars, China(30925023)+1 种基金the National Natural Science Foundation of China(30671297)the National High-Tech R&D Program of China(2009AA101102)
文摘Plant leaves respond to day/night cycling in a number of physiological ways. At the mRNA level, the expression of some genes changes during the 24 h period. To determine which proteins exhibited a rhythmic pattern of expression, proteomic profiles in maize seedling leaves were analyzed by high-throughput two-dimensional gel electrophoresis, combined with MALDI-TOF MS technology. Of the 464 proteins that were detected with silver staining in a pH range of 4-7, 17 （3.66%） showed clock rhythmicity in their abundance. These proteins belonged to diverse functional groups and proteins involved in photosynthesis and carbon metabolism were over-represented. These findings provide a new perspective on the relationship between the physiological functions of leaves and the clock rhythmic system.
基金supported by the National Key R&D Program of China(Grant No.2016YFD0101003)the Heilongjiang Provincial Outstanding Youth Science Foundation,China(Grant No.JC2017008)
文摘De-etiolation consists of a series of developmental and physiological changes that a plant undergoes in response to light.During this process light,an important environmental signal,triggers the inhibition of mesocotyl elongation and the production of photosynthetically active chloroplasts,and etiolated leaves transition from the"sink"stage to the"source"stage.De-etiolation has been extensively studied in maize(Zea mays L.).However,little is known about how this transition is regulated.In this study,we described a quantitative proteomic and phosphoproteomic atlas of the de-etiolation process in maize.We identified 16,420 proteins in proteome,among which 14,168 proteins were quantified.In addition,8746 phosphorylation sites within 3110 proteins were identified.From the combined proteomic and phosphoproteomic data,we identified a total of 17,436 proteins.Only 7.0%(998/14,168)of proteins significantly changed in abundance during de-etiolation.In contrast,26.6%of phosphorylated proteins exhibited significant changes in phosphorylation level;these included proteins involved in gene expression and homeostatic pathways and rate-limiting enzymes involved in photosynthetic light and carbon reactions.Based on phosphoproteomic analysis,34.0%(1057/3110)of phosphorylated proteins identified in this study contained more than 2 phosphorylation sites,and 37 proteins contained more than 16 phosphorylation sites,indicating that multi-phosphorylation is ubiquitous during the de-etiolation process.Our results suggest that plants might preferentially regulate the level of posttranslational modifications(PTMs)rather than protein abundance for adapting to changing environments.The study of PTMs could thus better reveal the regulation of de-etiolation.
