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作 者:张丹[1] 徐虹[1] 李莎[1] 许宗奇[1] 魏艳[1]
机构地区:[1]南京工业大学食品与轻工学院,南京210009
出 处:《生物加工过程》2011年第5期53-58,共6页Chinese Journal of Bioprocess Engineering
基 金:江苏省农业科技自主创新基金资助项目(CX(10)226);江苏省自然科学基金资助项目(BK2009357);江苏省高校自然科学重大基础研究资助项目(08KJA180001)
摘 要:克隆Bacillus subtilis NX-2中的聚谷氨酸合成酶基因pgsBCA并进行测序。应用生物信息学分析方法和工具对PgsB、PgsC、PgsA蛋白质的理化性质、跨膜区域、信号肽、细胞定位等进行分析和预测,并探讨它们的作用方式。结果表明:PgsB蛋白不含有跨膜区,它与ATP结合并催化ATP的水解,为PGA合成提供能量;PgsC蛋白保守性最高,其含有4个跨膜区域,是疏水性膜结合蛋白;PgsA为亲水性稳定蛋白,在N端存在1个跨膜区域。The pgsBCA genes, encoding a poly-y-glutamic acid (T-PGA) synthesis system of B. subtilis NX-2, were cloned and sequenced. The physical and chemical properties, transmembrane region, signal peptide, cellular localization of PgsB, PgsC, and PgsA proteins were analyzed and predicted by using bioinformatics methods. Results showed that the essential ATP hydrolysis was mainly catalyzed by the action of PgsB protein, without transmembrane regions. PgsC was hydrophobic and membrane-bound protein containing four transmembrane regions. The pgsC gene was the most conservative gene of pgsBCA genes. PgsA was hydrophilic and stable protein containing one transmembrane domain near its N terminus, which seemed likely for the elongation of T-PGA. This study was helpful for explaining functions of the components PgsB, PgsC and PgsA of T-PGA synthesis system.
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