南通大学学报:自然科学版
南通大學學報:自然科學版
남통대학학보:자연과학판
Journal of Nantong University (Natural Science Edition)
2012年
2期
41-46
,共6页
姚文娟%范文俊%许小乐%邓小昭%张伟
姚文娟%範文俊%許小樂%鄧小昭%張偉
요문연%범문준%허소악%산소소%장위
γ-聚谷氨酸%生物信息学%PgsBCA
γ-聚穀氨痠%生物信息學%PgsBCA
γ-취곡안산%생물신식학%PgsBCA
poly-γ-glutamic acid%bioinformatics%PgsBCA
利用ProtParam、TopPred、PredictProtein、PSORT-B Prediction、SWISS-MODEL等软件分别分析蛋白质的理化性质、跨膜区、二级结构、亚细胞定位、三维结构.结果显示:PgsB是亲水不稳定蛋白,通过豆蔻酰锚钩锚定于质膜上,催化作用需与ATP结合提供能量;PgsC是疏水稳定蛋白,通过4个跨膜区和多个豆蔻酰锚钩定位于质膜,具有酰胺化位点;PgsA是亲水稳定蛋白,通过N端一个跨膜区和豆蔻酰锚钩结合于质膜,具有多种磷酸化位点.说明γ-聚谷氨酸(Polyγ-glutamic acid,γ-PGA)合成酶系3个组分蛋白形成复合物定位于质膜上,其中PgsB在胞内催化γ-PGA合成,PgsC固定于质膜,连接PgsB和PgsA组分,PgsA在胞外负责γ-PGA的运输.通过对γ-PGA合成酶系各组分蛋白结构的分析,为日后在谷氨酸高产菌株中的表达奠定了基础.
利用ProtParam、TopPred、PredictProtein、PSORT-B Prediction、SWISS-MODEL等軟件分彆分析蛋白質的理化性質、跨膜區、二級結構、亞細胞定位、三維結構.結果顯示:PgsB是親水不穩定蛋白,通過豆蔻酰錨鉤錨定于質膜上,催化作用需與ATP結閤提供能量;PgsC是疏水穩定蛋白,通過4箇跨膜區和多箇豆蔻酰錨鉤定位于質膜,具有酰胺化位點;PgsA是親水穩定蛋白,通過N耑一箇跨膜區和豆蔻酰錨鉤結閤于質膜,具有多種燐痠化位點.說明γ-聚穀氨痠(Polyγ-glutamic acid,γ-PGA)閤成酶繫3箇組分蛋白形成複閤物定位于質膜上,其中PgsB在胞內催化γ-PGA閤成,PgsC固定于質膜,連接PgsB和PgsA組分,PgsA在胞外負責γ-PGA的運輸.通過對γ-PGA閤成酶繫各組分蛋白結構的分析,為日後在穀氨痠高產菌株中的錶達奠定瞭基礎.
이용ProtParam、TopPred、PredictProtein、PSORT-B Prediction、SWISS-MODEL등연건분별분석단백질적이화성질、과막구、이급결구、아세포정위、삼유결구.결과현시:PgsB시친수불은정단백,통과두구선묘구묘정우질막상,최화작용수여ATP결합제공능량;PgsC시소수은정단백,통과4개과막구화다개두구선묘구정위우질막,구유선알화위점;PgsA시친수은정단백,통과N단일개과막구화두구선묘구결합우질막,구유다충린산화위점.설명γ-취곡안산(Polyγ-glutamic acid,γ-PGA)합성매계3개조분단백형성복합물정위우질막상,기중PgsB재포내최화γ-PGA합성,PgsC고정우질막,련접PgsB화PgsA조분,PgsA재포외부책γ-PGA적운수.통과대γ-PGA합성매계각조분단백결구적분석,위일후재곡안산고산균주중적표체전정료기출.
The physico-chemical properties,trans-membrane domains,secondary structures,sub-cellular localization and spatial structures are studied by ProtParam,TopPred,PredictProtein,PSORT-B Prediction and SWISS-MODEL,respectively.The results show that PgsB is a protein of hydrophilia and instability,and localizes to the membrane by myristoyl anchors.The catalytic action of PgsB requires combination of ATP to provide energy;PgsC is hydrophobic and stable,and localizes to the membrane by four trans-membrane domains and myristoyl anchors.PgsC has an amidation motif.PgsA is hydrophilic and stable,and localizes to the membrane by a trans-membrane domain in N terminus and myristoyl anchors.PgsC has many phosphorylation motifs.The results demonstrate that the compound of the three constituents from γ-PGA synthetase system is localized to the membrane.PgsB catalyzes γ-PGA synthesis.PgsC links PgsB and PgsA in the membrane.PgsA transports γ-PGA outside the cell.This study analyzes the structures of constituents from poly-γ-glutamate(γ-PGA) synthetase system in order to benefit expression of the synthetase system in the glutamate-producing strain.