Interaction of the Pseudomonas cepacia DSM3959 lipase with its chaperone, LimA.
Interaction of the Pseudomonas cepacia DSM3959 lipase with its chaperone, LimA.
复制标题
洋葱假单胞菌 DSM3959 脂肪酶与其伴侣 LimA 的相互作用。
DOI：
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发表时间：
1995
期刊：
影响因子：
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通讯作者：
D. McConnell
中科院分区：
文献类型：
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作者：
A. Hobson;C. Buckley;S. Jørgensen;B. Diderichsen;D. McConnell
洋葱假单胞菌DSM 3959的利帕基因需要下游基因limA来表达脂肪酶活性。lim基因的产物LimA是脂肪酶折叠过程中所需的分子伴侣，以使脂肪酶采取活性构象。脂肪酶和LimA蛋白质已显示形成可与抗脂肪酶或抗LimA抗体沉淀的复合物。LimA与从“天然”洋葱假单胞菌系统中分离的前脂肪酶和脂肪酶形成1：1的复合物。成熟的脂肪酶（缺乏其信号肽）已在大肠杆菌中的LimA的存在和不存在下表达。在尿素变性-复性实验中，LimA可以激活成熟脂肪酶，表明LimA激活脂肪酶不需要信号肽。研究了不同试剂对8 M尿素复性脂肪酶的影响.我们提出了一种机制的LimA分子伴侣的功能在生产过程中的活性胞外脂肪酶。
The lipA gene of Pseudomonas cepacia DSM3959 requires a downstream gene, limA, in oder to express lipase activity. The product of the lim gene, LimA, is a molecular chaperone required during the folding of lipase in oder for the lipase to adopt an active conformation. The lipase and LimA proteins have been shown to form a complex precipitable with either an anti-lipase or anti-LimA antibody. LimA has been shown to form a 1:1 complex with with prelipase and lipase isolated from "natural" P. cepacia system. The mature lipase (lacking its signal peptide) has been expressed in the presence and absence of LimA in Escherichia coli. LimA can activate mature lipase during a urea denaturation-renaturation experiment, indicating that the signal peptide is not required for the lipase to be activated by LimA. The effects of various reagents on the renaturation of lipase from 8 M urea have been examined. We propose a mechanism for the function of the LimA chaperone during the production of active extracellular lipase.