Unity and diversity in active transport in cell membrans

It is important to analyze many transport systems for the investigation of unity and diversity in结构，功能和机制在主动传输proteins. Fortunately，我们已经找到并投资了积极主动的交通系统在基础设施cells so far. in the pasttwo大家,1)我们分析人员Na我们分析D1+ D1-coupled交通系统，mainly Na symporter and melibiose symporter and serine symporter of Escherichia coli and some其他bacteria.我们characterized the symporters from biochemical view point and genetic view point。我们established methods for over productionlarge-scale purification and reconstitution of the Na melibiose symporter protein andNa /serine symporter protein. This opened up a way for further analysis in structure，function and mechanism an active transport proteins.2) We identified regions and amino acid residuesimportant or necessary for ion-coupling or substrate recognition in the Na i - D1+ i - D1/melibioseHomology search and motif：系统搜索和模式分析系统，然后通过mutant analysis and site-directed mutagenesisanalysis were also useful for such analysis.3)我们发现了新的交通系统和cloned their genesin some bacteria . biochemical and genetic analyses further revealed unity and diversity intransport proteins.Collaborations with Prof. Wilson and Prof. Konings were very valuable foe thisfeed。

It is important to analyze many transport systems for the investigation of unity and diversity in structure, function and mechanism in active transport proteins. Fortunately, we have found and investigated many active transport systems in bacterial cells so far. In the past two years, we have obtained the following results.1) We analyzed many NaィイD1+ィエD1-coupled transport systems, mainly NaィイD1+ィエD1/melibiose symporter and NaィイD1+ィエD1/serine symporter of Escherichia coli and some other bacteria. We characterized the symporters from biochemical view point and genetic view point. We established methods for over production, large-scale purification and reconstitution of the NaィイD1+ィエD1/melibiose symporter protein and NaィイD1+ィエD1/serine symporter protein. This opened up a way for further analysis in structure, function and mechanism an active transport proteins.2) We identified regions and amino acid residues important or necessary for ion-coupling or substrate recognition in the NaィイD1+ィエD1/melibiose symporter protein through mutant analysis and site-directed mutagenesis. Homology search and motif analysis were also useful for such analysis.3) We found new transport systems and cloned their genes in some bacteria. Biochemical and genetic analyses further revealed unity and diversity in transport proteins.Collaborations with Prof. Wilson and Prof. Konings were very valuable foe this project.