运用还原论和整体论,剖析战争复杂性处理的一般思维:分解和综合.基于宏观尺度上指挥与控制(Command and Control,C2)活动的一般过程PREA环,分析体系作战复杂问题分解后的典型特征:多域性、并发性、异步性和冲突性,建立宏观作战体系C2活...运用还原论和整体论,剖析战争复杂性处理的一般思维:分解和综合.基于宏观尺度上指挥与控制(Command and Control,C2)活动的一般过程PREA环,分析体系作战复杂问题分解后的典型特征:多域性、并发性、异步性和冲突性,建立宏观作战体系C2活动内核框架.以宏观体系的稳定有序运行为目的,分析多域多环并发异步运行的冲突类型及冲突协调方法,建立宏观作战体系指挥控制过程多域多PREA环异步运行及冲突协调管理模型.以美海军航母打击大队指挥体制与指挥方式为例,运用冲突协调管理模型解释其科学性.基于多域多PREA环异步并发运行及冲突协调模型分析,提出宏观作战体系C2活动的指导.展开更多
Pollen fertility is a crucial factor for successful pollination and essential for seed formation. Recent studies have suggested that a diverse range of internal and external factors, signaling components and their rel...Pollen fertility is a crucial factor for successful pollination and essential for seed formation. Recent studies have suggested that a diverse range of internal and external factors, signaling components and their related pathways are likely involved in pollen fertility. Here, we report a single C2-domain containing protein, OsPBP1, initially identified through cDNA microarray analysis. OsPBP1 is a single copy gene and preferentially expressed in pistil and pollen but downregulated by pollination. OsPBP1 had a calcium concentration-dependent phospholipid-binding activity and was localized mainly in cytoplasm and nucleus, but translocated onto the plasma membrane in response to an intracellular Ca^2＋ increase. Pollen grains of antisense OsPBP1 transgenic lines were largely nonviable, germinated poorly in vitro and of low fertility. OsPBP1 protein was localized in a region peripheral to pollen wall and vesicles of elongating pollen tube, and its repressed expression reduced substantially this association and led to alteration of microfilament polymerization during pollen germination. Taken together, these results indicate that OsPBP1 is a novel functional C2-domain phospholipids-binding protein that is required for pollen fertility likely by regulating Ca^2＋ and phospholipid signaling pathways.展开更多
In this paper we report that the C2 domain of synaptotagmin I (syt I) could associate with lipid rafts of plasma membrane. We demonstrate that phosphatidylinositol 4,5-bisphosphate (PIP2) in the target membrane and Ca...In this paper we report that the C2 domain of synaptotagmin I (syt I) could associate with lipid rafts of plasma membrane. We demonstrate that phosphatidylinositol 4,5-bisphosphate (PIP2) in the target membrane and Ca2+ are the key factors to enhance the raft association of the C2 domain. We also found that the raft association of the C2 domain could be fulfilled by either C2A or C2B alone, suggesting that their raft association might be complementary. Finally, we indicate that destroying lipid rafts or blocking syt I-raft association could significantly reduce the Ca2+-driven release of glutamates. Our data indicate that the raft association of the C2 domain might play an important role in the regulated exocytosis.展开更多
The C2 domain originally referred to the second of four constant structural motifs in protein kinase C (PKC). Now this domain represents a large structural family sharing a homologous dimensional structure in many ...The C2 domain originally referred to the second of four constant structural motifs in protein kinase C (PKC). Now this domain represents a large structural family sharing a homologous dimensional structure in many proteins that play important roles in many organisms. The C2A domain is one of the two C2 domains of synaptotagmin I involved in the Ca 2+ regulation of exocytosis. This domain is mostly composed of β sheet except for a small fraction of α helix, and therefore provides an ideal model for a protein folding study. In this report, the unfolding equilibrium of the C2A domain in guanidine hydrochloride (GdnHCl) containing solutions has been studied using ultraviolet (UV) difference spectrum, fluorescence spectrum, size exclusion chromatography (SEC), and circular dichroism (CD) spectrum. The results suggest that unfolding of the C2A domain occurs as a two state process during GdnHCl titration. By examining the changes of both tertiary structure and secondary structure, no intermediates could be detected during this unfolding study. However, it has been found that the native state of the C2A domain has a large hydrophobic surface. This result suggests that as a fragment of a protein, the C2A domain itself may exist in a state with large hydrophobic surface. This hydrophobic surface may be the molecular basis for interaction between domains in the whole protein. Furthermore, the hydrophobic behavior may play a role during the oligomerization of synaptotagmin.展开更多
文摘运用还原论和整体论,剖析战争复杂性处理的一般思维:分解和综合.基于宏观尺度上指挥与控制(Command and Control,C2)活动的一般过程PREA环,分析体系作战复杂问题分解后的典型特征:多域性、并发性、异步性和冲突性,建立宏观作战体系C2活动内核框架.以宏观体系的稳定有序运行为目的,分析多域多环并发异步运行的冲突类型及冲突协调方法,建立宏观作战体系指挥控制过程多域多PREA环异步运行及冲突协调管理模型.以美海军航母打击大队指挥体制与指挥方式为例,运用冲突协调管理模型解释其科学性.基于多域多PREA环异步并发运行及冲突协调模型分析,提出宏观作战体系C2活动的指导.
文摘Pollen fertility is a crucial factor for successful pollination and essential for seed formation. Recent studies have suggested that a diverse range of internal and external factors, signaling components and their related pathways are likely involved in pollen fertility. Here, we report a single C2-domain containing protein, OsPBP1, initially identified through cDNA microarray analysis. OsPBP1 is a single copy gene and preferentially expressed in pistil and pollen but downregulated by pollination. OsPBP1 had a calcium concentration-dependent phospholipid-binding activity and was localized mainly in cytoplasm and nucleus, but translocated onto the plasma membrane in response to an intracellular Ca^2＋ increase. Pollen grains of antisense OsPBP1 transgenic lines were largely nonviable, germinated poorly in vitro and of low fertility. OsPBP1 protein was localized in a region peripheral to pollen wall and vesicles of elongating pollen tube, and its repressed expression reduced substantially this association and led to alteration of microfilament polymerization during pollen germination. Taken together, these results indicate that OsPBP1 is a novel functional C2-domain phospholipids-binding protein that is required for pollen fertility likely by regulating Ca^2＋ and phospholipid signaling pathways.
基金Supported by the National Natural Science Foundation of China (Grant Nos. 30670501 and 30628007)the National Basic Research Program of China (Grant No. 2004 CB720005)
文摘In this paper we report that the C2 domain of synaptotagmin I (syt I) could associate with lipid rafts of plasma membrane. We demonstrate that phosphatidylinositol 4,5-bisphosphate (PIP2) in the target membrane and Ca2+ are the key factors to enhance the raft association of the C2 domain. We also found that the raft association of the C2 domain could be fulfilled by either C2A or C2B alone, suggesting that their raft association might be complementary. Finally, we indicate that destroying lipid rafts or blocking syt I-raft association could significantly reduce the Ca2+-driven release of glutamates. Our data indicate that the raft association of the C2 domain might play an important role in the regulated exocytosis.
基金Supported by the National Key Basic Research Specific Foundation of China(No.G19990 75 6 0 7)
文摘The C2 domain originally referred to the second of four constant structural motifs in protein kinase C (PKC). Now this domain represents a large structural family sharing a homologous dimensional structure in many proteins that play important roles in many organisms. The C2A domain is one of the two C2 domains of synaptotagmin I involved in the Ca 2+ regulation of exocytosis. This domain is mostly composed of β sheet except for a small fraction of α helix, and therefore provides an ideal model for a protein folding study. In this report, the unfolding equilibrium of the C2A domain in guanidine hydrochloride (GdnHCl) containing solutions has been studied using ultraviolet (UV) difference spectrum, fluorescence spectrum, size exclusion chromatography (SEC), and circular dichroism (CD) spectrum. The results suggest that unfolding of the C2A domain occurs as a two state process during GdnHCl titration. By examining the changes of both tertiary structure and secondary structure, no intermediates could be detected during this unfolding study. However, it has been found that the native state of the C2A domain has a large hydrophobic surface. This result suggests that as a fragment of a protein, the C2A domain itself may exist in a state with large hydrophobic surface. This hydrophobic surface may be the molecular basis for interaction between domains in the whole protein. Furthermore, the hydrophobic behavior may play a role during the oligomerization of synaptotagmin.
